ID AGT2_RAT Reviewed; 512 AA. AC Q64565; O08616; Q642F1; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 2. DT 27-NOV-2024, entry version 157. DE RecName: Full=Alanine--glyoxylate aminotransferase 2, mitochondrial; DE Short=AGT 2; DE EC=2.6.1.44 {ECO:0000269|PubMed:2123486, ECO:0000269|PubMed:6803844}; DE AltName: Full=(R)-3-amino-2-methylpropionate--pyruvate transaminase; DE EC=2.6.1.40 {ECO:0000269|PubMed:10989446, ECO:0000269|PubMed:2393662, ECO:0000269|PubMed:6803844}; DE AltName: Full=Beta-ALAAT II {ECO:0000303|PubMed:2393662}; DE AltName: Full=Beta-alanine-pyruvate aminotransferase; DE EC=2.6.1.18 {ECO:0000269|PubMed:10989446}; DE AltName: Full=D-3-aminoisobutyrate-pyruvate aminotransferase {ECO:0000303|PubMed:2393662}; DE AltName: Full=D-AIBAT {ECO:0000303|PubMed:10989446}; DE AltName: Full=D-beta-aminoisobutyrate-pyruvate aminotransferase {ECO:0000303|PubMed:10989446}; DE Flags: Precursor; GN Name=Agxt2; Synonyms=Agt2; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=Wistar; TISSUE=Kidney; RX PubMed=7592550; DOI=10.1093/oxfordjournals.jbchem.a124787; RA Matsui-Lee I.S., Muragaki Y., Ideguchi T., Hase T., Tsuji M., Ooshima A., RA Okuno E., Kido R.; RT "Molecular cloning and sequencing of a cDNA encoding alanine-glyoxylate RT aminotransferase 2 from rat kidney."; RL J. Biochem. 117:856-862(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 40-57, FUNCTION, CATALYTIC RP ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND RP COFACTOR. RC STRAIN=Sprague-Dawley; TISSUE=Liver; RX PubMed=10989446; DOI=10.1016/s0076-6879(00)24247-x; RA Tamaki N., Sakata S.F., Matsuda K.; RT "Purification, properties, and sequencing of aminoisobutyrate RT aminotransferases from rat liver."; RL Methods Enzymol. 324:376-389(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=6803844; DOI=10.1016/0304-4165(82)90054-x; RA Okuno E., Minatogawa Y., Kido R.; RT "Co-purification of alanine-glyoxylate aminotransferase with 2- RT aminobutyrate aminotransferase in rat kidney."; RL Biochim. Biophys. Acta 715:97-104(1982). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RX PubMed=2393662; DOI=10.1016/0304-4165(90)90106-7; RA Ueno S., Sano A., Hineno T., Kondoh K., Mizuno T., Morino H., Kakimoto Y.; RT "Further studies on D-3-aminoisobutyrate-pyruvate aminotransferase."; RL Biochim. Biophys. Acta 1035:128-131(1990). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=2123486; DOI=10.1016/s0021-9258(17)45307-5; RA Ogawa T., Kimoto M., Sasaoka K.; RT "Dimethylarginine:pyruvate aminotransferase in rats. Purification, RT properties, and identity with alanine:glyoxylate aminotransferase 2."; RL J. Biol. Chem. 265:20938-20945(1990). CC -!- FUNCTION: Multifunctional aminotransferase with a broad substrate CC specifcity (PubMed:10989446, PubMed:2123486, PubMed:2393662, CC PubMed:6803844). Catalyzes the conversion of glyoxylate to glycine CC using alanine as the amino donor (PubMed:2123486, PubMed:6803844). CC Catalyzes metabolism of not L- but the D-isomer of D-beta- CC aminoisobutyric acid to generate 2-methyl-3-oxopropanoate and alanine CC (PubMed:10989446, PubMed:2393662, PubMed:6803844). Catalyzes the CC transfer of the amino group from beta-alanine to pyruvate to yield L- CC alanine and 3-oxopropanoate (PubMed:10989446). Can metabolize NG- CC monomethyl-L-arginine (NMMA), asymmetric NG,NG-dimethyl-L-arginine CC (ADMA) and symmetric NG,N'G-dimethyl-L-arginine (SDMA) CC (PubMed:2123486). ADMA is a potent inhibitor of nitric-oxide (NO) CC synthase, and this activity provides mechanism through which the kidney CC regulates blood pressure (By similarity). CC {ECO:0000250|UniProtKB:Q9BYV1, ECO:0000269|PubMed:10989446, CC ECO:0000269|PubMed:2123486, ECO:0000269|PubMed:2393662, CC ECO:0000269|PubMed:6803844}. CC -!- CATALYTIC ACTIVITY: CC Reaction=glyoxylate + L-alanine = glycine + pyruvate; CC Xref=Rhea:RHEA:24248, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655, CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57972; EC=2.6.1.44; CC Evidence={ECO:0000269|PubMed:2123486, ECO:0000269|PubMed:6803844}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24249; CC Evidence={ECO:0000305|PubMed:6803844}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3- CC oxopropanoate + L-alanine; Xref=Rhea:RHEA:18393, ChEBI:CHEBI:15361, CC ChEBI:CHEBI:57700, ChEBI:CHEBI:57731, ChEBI:CHEBI:57972; EC=2.6.1.40; CC Evidence={ECO:0000269|PubMed:10989446, ECO:0000269|PubMed:2393662, CC ECO:0000269|PubMed:6803844}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18394; CC Evidence={ECO:0000305|PubMed:10989446}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxopropanoate + L-alanine = beta-alanine + pyruvate; CC Xref=Rhea:RHEA:14077, ChEBI:CHEBI:15361, ChEBI:CHEBI:33190, CC ChEBI:CHEBI:57966, ChEBI:CHEBI:57972; EC=2.6.1.18; CC Evidence={ECO:0000269|PubMed:10989446}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14079; CC Evidence={ECO:0000305|PubMed:10989446}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxobutanoate + L-alanine = (2S)-2-aminobutanoate + pyruvate; CC Xref=Rhea:RHEA:77355, ChEBI:CHEBI:15361, ChEBI:CHEBI:16763, CC ChEBI:CHEBI:57972, ChEBI:CHEBI:74359; EC=2.6.1.44; CC Evidence={ECO:0000269|PubMed:2123486}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(omega),N(omega)-dimethyl-L-arginine + pyruvate = 5-(3,3- CC dimethylguanidino)-2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77303, CC ChEBI:CHEBI:15361, ChEBI:CHEBI:57972, ChEBI:CHEBI:58326, CC ChEBI:CHEBI:197301; Evidence={ECO:0000269|PubMed:2123486}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(omega),N('omega)-dimethyl-L-arginine + pyruvate = 5-(3,3'- CC dimethylguanidino)-2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77307, CC ChEBI:CHEBI:15361, ChEBI:CHEBI:57972, ChEBI:CHEBI:197308, CC ChEBI:CHEBI:197310; Evidence={ECO:0000269|PubMed:2123486}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(omega),N(omega)-dimethyl-L-arginine + glyoxylate = 5-(3,3- CC dimethylguanidino)-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77311, CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:58326, CC ChEBI:CHEBI:197301; Evidence={ECO:0000269|PubMed:2123486}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(omega),N('omega)-dimethyl-L-arginine + glyoxylate = 5-(3,3'- CC dimethylguanidino)-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77315, CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:197308, CC ChEBI:CHEBI:197310; Evidence={ECO:0000269|PubMed:2123486}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(omega)-methyl-L-arginine + pyruvate = 5-(3-methylguanidino)- CC 2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77319, ChEBI:CHEBI:15361, CC ChEBI:CHEBI:57972, ChEBI:CHEBI:114953, ChEBI:CHEBI:197314; CC Evidence={ECO:0000269|PubMed:2123486}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(omega)-methyl-L-arginine + glyoxylate = 5-(3- CC methylguanidino)-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77323, CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:114953, CC ChEBI:CHEBI:197314; Evidence={ECO:0000269|PubMed:2123486}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-ornithine + pyruvate = 5-amino-2-oxopentanoate + L-alanine; CC Xref=Rhea:RHEA:77327, ChEBI:CHEBI:15361, ChEBI:CHEBI:46911, CC ChEBI:CHEBI:57972, ChEBI:CHEBI:58802; CC Evidence={ECO:0000269|PubMed:2123486}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-ornithine + glyoxylate = 5-amino-2-oxopentanoate + glycine; CC Xref=Rhea:RHEA:77331, ChEBI:CHEBI:36655, ChEBI:CHEBI:46911, CC ChEBI:CHEBI:57305, ChEBI:CHEBI:58802; CC Evidence={ECO:0000269|PubMed:2123486}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2S)-2-aminobutanoate + glyoxylate = 2-oxobutanoate + glycine; CC Xref=Rhea:RHEA:77339, ChEBI:CHEBI:16763, ChEBI:CHEBI:36655, CC ChEBI:CHEBI:57305, ChEBI:CHEBI:74359; CC Evidence={ECO:0000269|PubMed:2123486}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(omega),N(omega)-dimethyl-L-arginine + oxaloacetate = 5-(3,3- CC dimethylguanidino)-2-oxopentanoate + L-aspartate; CC Xref=Rhea:RHEA:77343, ChEBI:CHEBI:16452, ChEBI:CHEBI:29991, CC ChEBI:CHEBI:58326, ChEBI:CHEBI:197301; CC Evidence={ECO:0000269|PubMed:2123486}; CC -!- CATALYTIC ACTIVITY: CC Reaction=oxaloacetate + L-alanine = L-aspartate + pyruvate; CC Xref=Rhea:RHEA:77347, ChEBI:CHEBI:15361, ChEBI:CHEBI:16452, CC ChEBI:CHEBI:29991, ChEBI:CHEBI:57972; CC Evidence={ECO:0000269|PubMed:2123486}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(omega),N(omega)-dimethyl-L-arginine + 2-oxobutanoate = 5- CC (3,3-dimethylguanidino)-2-oxopentanoate + (2S)-2-aminobutanoate; CC Xref=Rhea:RHEA:77351, ChEBI:CHEBI:16763, ChEBI:CHEBI:58326, CC ChEBI:CHEBI:74359, ChEBI:CHEBI:197301; CC Evidence={ECO:0000269|PubMed:2123486}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxopentanoate + N(omega),N(omega)-dimethyl-L-arginine = 5- CC (3,3-dimethylguanidino)-2-oxopentanoate + L-2-aminopentanoate; CC Xref=Rhea:RHEA:77359, ChEBI:CHEBI:28644, ChEBI:CHEBI:58326, CC ChEBI:CHEBI:58441, ChEBI:CHEBI:197301; CC Evidence={ECO:0000269|PubMed:2123486}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxohexanoate + N(omega),N(omega)-dimethyl-L-arginine = L-2- CC aminohexanoate + 5-(3,3-dimethylguanidino)-2-oxopentanoate; CC Xref=Rhea:RHEA:77363, ChEBI:CHEBI:35177, ChEBI:CHEBI:58326, CC ChEBI:CHEBI:58455, ChEBI:CHEBI:197301; CC Evidence={ECO:0000269|PubMed:2123486}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000269|PubMed:10989446, ECO:0000269|PubMed:2123486}; CC -!- ACTIVITY REGULATION: Inhibited by 5-fluorouracil and 6-fluorouracil CC (PubMed:10989446). Inhibited by phenylhydrazine, hydroxylamine, l- CC amino-L-proline, para-chloromercuribenzoate and HgCl2 (PubMed:2123486). CC {ECO:0000269|PubMed:10989446, ECO:0000269|PubMed:2123486}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.12 mM for D-beta-aminoisobutyrate {ECO:0000269|PubMed:10989446}; CC KM=1.4 mM for beta-alanine {ECO:0000269|PubMed:10989446}; CC KM=13.7 uM for N(omega),N('omega)-dimethyl-L-arginine (with pyruvate CC as cosubstrate) {ECO:0000269|PubMed:2123486}; CC KM=11.1 uM for N(omega),N('omega)-dimethyl-L-arginine (with CC glyoxylate as cosubstrate) {ECO:0000269|PubMed:2123486}; CC KM=9.7 uM for N(omega),N(omega)-dimethyl-L-arginine (with pyruvate as CC cosubstrate) {ECO:0000269|PubMed:2123486}; CC KM=8 uM for N(omega)-methyl-L-arginine (with pyruvate as cosubstrate) CC {ECO:0000269|PubMed:2123486}; CC KM=70 uM for L-ornithine (with pyruvate as cosubstrate) CC {ECO:0000269|PubMed:2123486}; CC KM=7.8 uM for L-alanine (with glyoxylate as cosubstrate) CC {ECO:0000269|PubMed:2123486}; CC KM=2.2 uM for pyruvate (with N(omega),N('omega)-dimethyl-L-arginine CC as cosubstrate) {ECO:0000269|PubMed:2123486}; CC KM=2.4 uM for pyruvate (with N(omega),N(omega)-dimethyl-L-arginine as CC cosubstrate) {ECO:0000269|PubMed:2123486}; CC KM=2.5 uM for pyruvate (with N(omega)-methyl-L-arginine as CC cosubstrate) {ECO:0000269|PubMed:2123486}; CC KM=4.1 uM for pyruvate (with L-ornithine as cosubstrate) CC {ECO:0000269|PubMed:2123486}; CC KM=2.9 uM for glyoxylate (with L-alanine as cosubstrate) CC {ECO:0000269|PubMed:2123486}; CC KM=2.1 uM for glyoxylate (with N(omega),N('omega)-dimethyl-L-arginine CC as cosubstrate) {ECO:0000269|PubMed:2123486}; CC pH dependence: CC Optimum pH is 9.5 for transamination between L-alanine and CC glyoxylate. Optimum pH is 10.0 for the transamination between CC dimethylarginines and pyruvate. Optimum pH is 10.5 for the CC transamination between L-ornithine and pyruvate. CC {ECO:0000269|PubMed:10989446, ECO:0000269|PubMed:2123486}; CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10989446, CC ECO:0000269|PubMed:2123486}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:2123486, CC ECO:0000269|PubMed:2393662}. CC -!- TISSUE SPECIFICITY: Expressed in the liver, lung and kidney. CC {ECO:0000269|PubMed:2123486, ECO:0000269|PubMed:2393662}. CC -!- DEVELOPMENTAL STAGE: Expression is low at birth, increases sharply CC thereafter for 10 days, and then subsequently declines to the adult CC level. {ECO:0000269|PubMed:2393662}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D38100; BAA07281.1; -; mRNA. DR EMBL; AB002584; BAA19549.1; -; mRNA. DR EMBL; BC081765; AAH81765.1; -; mRNA. DR RefSeq; NP_114023.1; NM_031835.2. DR AlphaFoldDB; Q64565; -. DR SMR; Q64565; -. DR STRING; 10116.ENSRNOP00000024035; -. DR iPTMnet; Q64565; -. DR PhosphoSitePlus; Q64565; -. DR PaxDb; 10116-ENSRNOP00000024035; -. DR Ensembl; ENSRNOT00000024035.8; ENSRNOP00000024035.5; ENSRNOG00000017821.8. DR Ensembl; ENSRNOT00055046650; ENSRNOP00055038288; ENSRNOG00055026998. DR Ensembl; ENSRNOT00060035993; ENSRNOP00060029618; ENSRNOG00060020703. DR GeneID; 83784; -. DR KEGG; rno:83784; -. DR AGR; RGD:621767; -. DR CTD; 64902; -. DR RGD; 621767; Agxt2. DR eggNOG; KOG1404; Eukaryota. DR GeneTree; ENSGT00940000156125; -. DR HOGENOM; CLU_016922_8_0_1; -. DR InParanoid; Q64565; -. DR OMA; MVPGFKY; -. DR OrthoDB; 345661at2759; -. DR BRENDA; 2.6.1.40; 5301. DR BRENDA; 2.6.1.44; 5301. DR Reactome; R-RNO-389661; Glyoxylate metabolism and glycine degradation. DR SABIO-RK; Q64565; -. DR PRO; PR:Q64565; -. DR Proteomes; UP000002494; Chromosome 2. DR Bgee; ENSRNOG00000017821; Expressed in adult mammalian kidney and 11 other cell types or tissues. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0047305; F:(R)-3-amino-2-methylpropionate-pyruvate transaminase activity; IDA:UniProtKB. DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IDA:UniProtKB. DR GO; GO:0016223; F:beta-alanine-pyruvate transaminase activity; IDA:UniProtKB. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; ISO:RGD. DR GO; GO:0009436; P:glyoxylate catabolic process; ISO:RGD. DR GO; GO:0019481; P:L-alanine catabolic process, by transamination; ISO:RGD. DR GO; GO:2001299; P:N(omega),N(omega)-dimethyl-L-arginine catabolic process; IDA:UniProtKB. DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:RGD. DR CDD; cd00610; OAT_like; 1. DR FunFam; 3.40.640.10:FF:000055; Alanine--glyoxylate aminotransferase 2, mitochondrial; 1. DR FunFam; 3.90.1150.10:FF:000105; alanine--glyoxylate aminotransferase 2, mitochondrial isoform X3; 1. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR049704; Aminotrans_3_PPA_site. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1. DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 1: Evidence at protein level; KW Acetylation; Aminotransferase; Direct protein sequencing; Mitochondrion; KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide. FT TRANSIT 1..39 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:10989446" FT CHAIN 40..512 FT /note="Alanine--glyoxylate aminotransferase 2, FT mitochondrial" FT /id="PRO_0000001270" FT MOD_RES 55 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q3UEG6" FT MOD_RES 69 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q3UEG6" FT MOD_RES 69 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q3UEG6" FT MOD_RES 82 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q3UEG6" FT MOD_RES 260 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q3UEG6" FT MOD_RES 260 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q3UEG6" FT MOD_RES 302 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q3UEG6" FT MOD_RES 348 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000250" FT MOD_RES 415 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q3UEG6" FT MOD_RES 415 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q3UEG6" FT MOD_RES 418 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q3UEG6" FT MOD_RES 418 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q3UEG6" FT MOD_RES 452 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q3UEG6" FT CONFLICT 305 FT /note="F -> L (in Ref. 1; BAA07281)" FT /evidence="ECO:0000305" FT CONFLICT 332 FT /note="W -> Y (in Ref. 1; BAA07281)" FT /evidence="ECO:0000305" FT CONFLICT 337..338 FT /note="HD -> QA (in Ref. 1; BAA07281)" FT /evidence="ECO:0000305" FT CONFLICT 435..436 FT /note="MV -> WW (in Ref. 1; BAA07281)" FT /evidence="ECO:0000305" FT CONFLICT 494..496 FT /note="FAF -> LAL (in Ref. 1; BAA07281)" FT /evidence="ECO:0000305" SQ SEQUENCE 512 AA; 57201 MW; C35E389789516B5C CRC64; MSLAWRTLQK AFYLETSLRI LQMRPSLSCA SRIYVPKLTL HTKHNMPPCD FSPEKYQSLA YNHVLEIHKQ HLSPVNTAYF QKPLLLHQGH MEWLFDSEGN RYLDFFSGIV TVGVGHCHPK VTAVAKKQMD RLWHTSSVFF HSPMHEYAER LSALLPEPLK VIFLVNSGSE ANDLAMVMAR AYSNHTDIIS FRGAYHGCSP YTLGLTNVGI YKMKVPSTIA CQSTMCPDVF RGPWGGSHCR DSPVQTVRKC SCAPDGCQAK ERYIEQFKDT LNTSVATSIA GFFAEPIQGV NGVVQYPKEF LKEAFALVRE RGGVCIADEV QTGFGRLGSH FWGFQTHDTM PDIVTMAKGI GNGFPMAAVV TTPEIASSLA KHLHHFSTFG GSPLACAIGS AVLEVIEEEN LQRNSQEVGT YMLLKFAKLR DEFDIVGDVR GKGLMVGIEM VQDKISRQPL PKTEVNQIHE DCKDMGLLVG RGGNFSQTFR IAPPMRVTKL EVDFAFEVFR SALTQHMERR AK // ID METW_YEAST Reviewed; 575 AA. AC Q12198; D6VXV0; DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-NOV-2024, entry version 156. DE RecName: Full=Homocysteine/cysteine synthase {ECO:0000250|UniProtKB:P06106}; DE EC=2.5.1.47 {ECO:0000269|PubMed:36455053}; DE EC=2.5.1.49 {ECO:0000269|PubMed:36379252, ECO:0000269|PubMed:36455053}; DE AltName: Full=Hydrogen sulfide utilizing 1 {ECO:0000303|PubMed:36455053}; DE AltName: Full=O-acetylserine/O-acetylhomoserine sulfhydrylase {ECO:0000250|UniProtKB:P06106}; DE Short=OAS-OAH SHLase {ECO:0000250|UniProtKB:P06106}; DE Short=OAS-OAH sulfhydrylase {ECO:0000250|UniProtKB:P06106}; GN Name=HSU1 {ECO:0000303|PubMed:36455053}; GN OrderedLocusNames=YLL058W {ECO:0000312|SGD:S000003981}; GN ORFNames=L0569 {ECO:0000312|SGD:S000003981}; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RA Wedler H., Wambutt R.; RT "Sequence of a 37 kb DNA fragment from chromosome XII of Saccharomyces RT cerevisiae including the subtelomeric region of the left arm."; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169871; DOI=10.1038/387s087; RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., RA Zollner A., Hani J., Hoheisel J.D.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; RL Nature 387:87-90(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-376. RX PubMed=36379252; DOI=10.1016/j.jbc.2022.102697; RA Van Oss S.B., Parikh S.B., Coelho N.C., Wacholder A., Belashov I., RA Zdancewicz S., Michaca M., Xu J., Kang Y.P., Ward N.P., Yoon S.J., RA McCourt K.M., McKee J., Ideker T., VanDemark A.P., DeNicola G.M., RA Carvunis A.R.; RT "On the illusion of auxotrophy: met15Delta yeast cells can grow on RT inorganic sulfur thanks to the previously uncharacterized homocysteine RT synthase Yll058w."; RL J. Biol. Chem. 298:102697-102697(2022). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=36455053; DOI=10.1371/journal.pbio.3001912; RA Yu J.S.L., Heineike B.M., Hartl J., Aulakh S.K., Correia-Melo C., RA Lehmann A., Lemke O., Agostini F., Lee C.T., Demichev V., Messner C.B., RA Muelleder M., Ralser M.; RT "Inorganic sulfur fixation via a new homocysteine synthase allows yeast RT cells to cooperatively compensate for methionine auxotrophy."; RL PLoS Biol. 20:e3001912-e3001912(2022). CC -!- FUNCTION: Plays a role in inorganic sulfur assimilation during sulfur- CC limited conditions; catalyzes the conversion of O-acetyl-L-homoserine CC (OAH) into homocysteine in the methionine biosynthesis pathway CC (PubMed:36379252, PubMed:36455053). Also catalyzes the conversion of O- CC acetylserine (OAS) into cysteine, the last step in the cysteine CC biosynthesis pathway (PubMed:36455053). However, it seems that in CC S.cerevisiae cysteine biosynthesis occurs exclusively through the CC cystathionine pathway and not via direct incorporation of sulfur into CC OAS (By similarity). It therefore has no metabolic role in cysteine CC biosynthesis and may only have a regulatory role controlling OAS levels CC (By similarity). {ECO:0000250|UniProtKB:P06106, CC ECO:0000269|PubMed:36379252, ECO:0000269|PubMed:36455053}. CC -!- CATALYTIC ACTIVITY: CC Reaction=O-acetyl-L-homoserine + methanethiol = L-methionine + acetate CC + H(+); Xref=Rhea:RHEA:10048, ChEBI:CHEBI:15378, ChEBI:CHEBI:16007, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:57716, ChEBI:CHEBI:57844; EC=2.5.1.49; CC Evidence={ECO:0000250|UniProtKB:P06106}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O-acetyl-L-homoserine + hydrogen sulfide = L-homocysteine + CC acetate; Xref=Rhea:RHEA:27822, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089, CC ChEBI:CHEBI:57716, ChEBI:CHEBI:58199; EC=2.5.1.49; CC Evidence={ECO:0000269|PubMed:36379252, ECO:0000269|PubMed:36455053}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate; CC Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089, CC ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47; CC Evidence={ECO:0000269|PubMed:36455053}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250|UniProtKB:P06106}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=4.29 uM for O-acetyl-L-homoserine (OAH) (at 30 degrees Celsius in CC potassium phosphate buffer) {ECO:0000269|PubMed:36379252}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo CC pathway; L-homocysteine from O-acetyl-L-homoserine. CC {ECO:0000305|PubMed:36379252, ECO:0000305|PubMed:36455053}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06106}. CC -!- INDUCTION: Induced in sulfur-limiting conditions (at protein level). CC {ECO:0000269|PubMed:36455053}. CC -!- DISRUPTION PHENOTYPE: Decreases growth during sulfur-limited conditions CC (PubMed:36455053). Simultaneous knockout of MET17 results in an CC inability to utilize hydrogen sulfide for methionine metabolism, and CC toxic accumulation of hydrogen sulfide (PubMed:36379252, CC PubMed:36455053). {ECO:0000269|PubMed:36379252, CC ECO:0000269|PubMed:36455053}. CC -!- MISCELLANEOUS: Present with 2070 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family. MET7 CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z47973; CAA87999.1; -; Genomic_DNA. DR EMBL; Z73163; CAA97511.1; -; Genomic_DNA. DR EMBL; BK006945; DAA09266.1; -; Genomic_DNA. DR PIR; S50962; S50962. DR RefSeq; NP_013042.1; NM_001181878.1. DR AlphaFoldDB; Q12198; -. DR SMR; Q12198; -. DR BioGRID; 31257; 52. DR STRING; 4932.YLL058W; -. DR PaxDb; 4932-YLL058W; -. DR PeptideAtlas; Q12198; -. DR EnsemblFungi; YLL058W_mRNA; YLL058W; YLL058W. DR GeneID; 850668; -. DR KEGG; sce:YLL058W; -. DR AGR; SGD:S000003981; -. DR SGD; S000003981; YLL058W. DR VEuPathDB; FungiDB:YLL058W; -. DR eggNOG; KOG0053; Eukaryota. DR GeneTree; ENSGT00940000176383; -. DR HOGENOM; CLU_011302_1_0_1; -. DR InParanoid; Q12198; -. DR OMA; LACPYVH; -. DR OrthoDB; 35837at2759; -. DR BioCyc; YEAST:G3O-32157-MONOMER; -. DR BioGRID-ORCS; 850668; 3 hits in 10 CRISPR screens. DR PRO; PR:Q12198; -. DR Proteomes; UP000002311; Chromosome XII. DR RNAct; Q12198; protein. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IBA:GO_Central. DR GO; GO:0004124; F:cysteine synthase activity; IEA:RHEA. DR GO; GO:0003961; F:O-acetylhomoserine aminocarboxypropyltransferase activity; IDA:UniProtKB. DR GO; GO:0051009; F:O-acetylhomoserine sulfhydrylase activity; IEA:RHEA. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0071269; P:L-homocysteine biosynthetic process; IDA:UniProtKB. DR GO; GO:0000103; P:sulfate assimilation; IMP:UniProtKB. DR GO; GO:0006790; P:sulfur compound metabolic process; IMP:SGD. DR GO; GO:0006791; P:sulfur utilization; IMP:UniProtKB. DR GO; GO:0019346; P:transsulfuration; IBA:GO_Central. DR FunFam; 3.90.1150.10:FF:000063; Probable cystathionine gamma-synthase; 1. DR FunFam; 3.40.640.10:FF:000175; YLL058W-like protein; 1. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR InterPro; IPR051750; Trans-sulfuration_enzymes. DR PANTHER; PTHR42699; -; 1. DR PANTHER; PTHR42699:SF1; CYSTATHIONINE GAMMA-SYNTHASE-RELATED; 1. DR Pfam; PF01053; Cys_Met_Meta_PP; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Cytoplasm; Methionine biosynthesis; KW Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1..575 FT /note="Homocysteine/cysteine synthase" FT /id="PRO_0000114782" FT MOD_RES 376 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000250|UniProtKB:P06721" FT MUTAGEN 376 FT /note="K->A: Abolishes catalytic activity." FT /evidence="ECO:0000269|PubMed:36379252" SQ SEQUENCE 575 AA; 64223 MW; EDE6292C60ADFDC1 CRC64; MTEIEFGQPL PSNLDYAVSF GIPTWDSAIG YAEKVPEVIG KMATGYPRYF PQPPVQRLCA YFVKKFGRGS ENCRPFPSVN LGLKCFEYVK SVSGPESKAH LEVETVTIKN RGAKTSKEPA ELVLTIAAVL ASEEEFETVK EYWKLRGECV SSRLALSVNQ LLDCANHGSE QVLRELEAGV FAAKKGEEKA KNLIKGRIVE NRFRPFGLEK KTPNWEGLNL NPNEDVYLVS SGMSAISTAR NLLTFWEEKK NSGDSLNKTT SDQKKKPLLC DTVGIFGFPF KDTQVIMTKF GKCKFFGFGN SRDVVELQKF LETSKQRILA VFVETPSNPL LNMPDLKKLR SLADQYGFFI VIDDTIGGLN VDILPYADIV STSLTKLFNG ASNVMGGSVV LNPKSSLYPY AREYFRSANF EDLLWCEDAI VLERNSRDFE DRTLRANANT GILLNDLLLP EEGKICKKIY YPTVTSKETF ENYESVRNER GGYGCLFSVA FFNEGDAKAF YDSLKVFKGP SNGTNFTLAC PYVHLAHHSE LEEVSKFGAD PNIIRVSVGL EDIQWLLKVF SSALDVVKSR GSKHS // ID ARGD_ECOLI Reviewed; 406 AA. AC P18335; Q2M725; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-NOV-2024, entry version 193. DE RecName: Full=Acetylornithine/succinyldiaminopimelate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000305}; DE Short=ACOAT {ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000303|PubMed:2199330}; DE Short=DapATase {ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000303|PubMed:10074354}; DE Short=Succinyldiaminopimelate transferase {ECO:0000255|HAMAP-Rule:MF_01107}; DE EC=2.6.1.11 {ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000269|PubMed:10074354}; DE EC=2.6.1.17 {ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000269|PubMed:10074354}; GN Name=argD {ECO:0000255|HAMAP-Rule:MF_01107}; GN Synonyms=dapC {ECO:0000255|HAMAP-Rule:MF_01107}, dtu; GN OrderedLocusNames=b3359, JW3322; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2199330; DOI=10.1016/0378-1119(90)90440-3; RA Heimberg H., Boyen A., Crabeel M., Glansdorff N.; RT "Escherichia coli and Saccharomyces cerevisiae acetylornithine RT aminotransferase: evolutionary relationship with ornithine RT aminotransferase."; RL Gene 90:69-78(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [4] RP PROTEIN SEQUENCE OF 2-13. RC STRAIN=K12 / EMG2; RX PubMed=9298646; DOI=10.1002/elps.1150180807; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded in the RT genome of Escherichia coli K-12."; RL Electrophoresis 18:1259-1313(1997). RN [5] RP PROTEIN SEQUENCE OF 2-27 AND 69-77, FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND PATHWAY. RX PubMed=10074354; DOI=10.1021/bi982574a; RA Ledwidge R., Blanchard J.S.; RT "The dual biosynthetic capability of N-acetylornithine aminotransferase in RT arginine and lysine biosynthesis."; RL Biochemistry 38:3019-3024(1999). CC -!- FUNCTION: Involved in both the arginine and lysine biosynthetic CC pathways. {ECO:0000255|HAMAP-Rule:MF_01107, CC ECO:0000269|PubMed:10074354}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L- CC glutamate 5-semialdehyde + L-glutamate; Xref=Rhea:RHEA:18049, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:57805; EC=2.6.1.11; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01107, ECO:0000269|PubMed:10074354}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N-succinyl-(2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = CC (S)-2-succinylamino-6-oxoheptanedioate + L-glutamate; CC Xref=Rhea:RHEA:11960, ChEBI:CHEBI:15685, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58087; EC=2.6.1.17; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01107, CC ECO:0000269|PubMed:10074354}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01107, CC ECO:0000305|PubMed:10074354}; CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01107, ECO:0000305|PubMed:10074354}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.15 mM for N-acetylornithine {ECO:0000269|PubMed:10074354}; CC KM=0.075 mM for N-succinyldiaminopimelate CC {ECO:0000269|PubMed:10074354}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl- CC L-ornithine from L-glutamate: step 4/4. {ECO:0000255|HAMAP- CC Rule:MF_01107, ECO:0000305|PubMed:10074354}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate CC (succinylase route): step 2/3. {ECO:0000255|HAMAP-Rule:MF_01107, CC ECO:0000305|PubMed:10074354}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01107}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01107, CC ECO:0000305}. CC -!- MISCELLANEOUS: The reaction catalyzed by ACOAT is highly reversible. CC This enzyme may also transaminate ornithine. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. ArgD subfamily. {ECO:0000255|HAMAP- CC Rule:MF_01107, ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M32796; AAA23480.1; -; Genomic_DNA. DR EMBL; U18997; AAA58156.1; -; Genomic_DNA. DR EMBL; U00096; AAC76384.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77931.1; -; Genomic_DNA. DR PIR; B65130; B65130. DR RefSeq; NP_417818.1; NC_000913.3. DR RefSeq; WP_000963792.1; NZ_SSZK01000008.1. DR AlphaFoldDB; P18335; -. DR SMR; P18335; -. DR BioGRID; 4260742; 10. DR DIP; DIP-9138N; -. DR IntAct; P18335; 6. DR STRING; 511145.b3359; -. DR jPOST; P18335; -. DR PaxDb; 511145-b3359; -. DR EnsemblBacteria; AAC76384; AAC76384; b3359. DR GeneID; 947864; -. DR KEGG; ecj:JW3322; -. DR KEGG; eco:b3359; -. DR KEGG; ecoc:C3026_18245; -. DR PATRIC; fig|1411691.4.peg.3371; -. DR EchoBASE; EB0064; -. DR eggNOG; COG4992; Bacteria. DR HOGENOM; CLU_016922_10_1_6; -. DR InParanoid; P18335; -. DR OMA; RSAWDLC; -. DR OrthoDB; 9801052at2; -. DR PhylomeDB; P18335; -. DR BioCyc; EcoCyc:ACETYLORNTRANSAM-MONOMER; -. DR BioCyc; MetaCyc:ACETYLORNTRANSAM-MONOMER; -. DR UniPathway; UPA00034; UER00020. DR UniPathway; UPA00068; UER00109. DR PRO; PR:P18335; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central. DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IDA:EcoliWiki. DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc. DR GO; GO:0009016; F:succinyldiaminopimelate transaminase activity; IDA:EcoCyc. DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IGI:EcoCyc. DR GO; GO:0033359; P:lysine biosynthetic process via diaminopimelate and N-succinyl-2-amino-6-ketopimelate; IGI:EcoCyc. DR CDD; cd00610; OAT_like; 1. DR FunFam; 3.40.640.10:FF:000004; Acetylornithine aminotransferase; 1. DR FunFam; 3.90.1150.10:FF:000009; Succinylornithine transaminase; 1. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR HAMAP; MF_01107; ArgD_aminotrans_3; 1. DR InterPro; IPR017652; Ac/SucOrn_transaminase_bac. DR InterPro; IPR004636; AcOrn/SuccOrn_fam. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR049704; Aminotrans_3_PPA_site. DR InterPro; IPR050103; Class-III_PLP-dep_AT. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR NCBIfam; TIGR03246; arg_catab_astC; 1. DR NCBIfam; TIGR00707; argD; 1. DR PANTHER; PTHR11986:SF113; ACETYLORNITHINE_SUCCINYLDIAMINOPIMELATE AMINOTRANSFERASE; 1. DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis; KW Cytoplasm; Direct protein sequencing; Lysine biosynthesis; KW Pyridoxal phosphate; Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:10074354, FT ECO:0000269|PubMed:9298646" FT CHAIN 2..406 FT /note="Acetylornithine/succinyldiaminopimelate FT aminotransferase" FT /id="PRO_0000112743" FT BINDING 108..109 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000250|UniProtKB:P40732, ECO:0000255|HAMAP- FT Rule:MF_01107" FT BINDING 141 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000250|UniProtKB:P40732, ECO:0000255|HAMAP- FT Rule:MF_01107" FT BINDING 144 FT /ligand="N(2)-acetyl-L-ornithine" FT /ligand_id="ChEBI:CHEBI:57805" FT /evidence="ECO:0000250|UniProtKB:Q5SHH5, ECO:0000255|HAMAP- FT Rule:MF_01107" FT BINDING 226..229 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000250|UniProtKB:P40732, ECO:0000255|HAMAP- FT Rule:MF_01107" FT BINDING 283 FT /ligand="N(2)-acetyl-L-ornithine" FT /ligand_id="ChEBI:CHEBI:57805" FT /evidence="ECO:0000250|UniProtKB:Q5SHH5, ECO:0000255|HAMAP- FT Rule:MF_01107" FT BINDING 284 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000250|UniProtKB:P40732, ECO:0000255|HAMAP- FT Rule:MF_01107" FT MOD_RES 255 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000250|UniProtKB:P40732, ECO:0000255|HAMAP- FT Rule:MF_01107" FT CONFLICT 245..247 FT /note="GVT -> ALA (in Ref. 1; AAA23480)" FT /evidence="ECO:0000305" SQ SEQUENCE 406 AA; 43767 MW; 645AA1EBCA442214 CRC64; MAIEQTAITR ATFDEVILPI YAPAEFIPVK GQGSRIWDQQ GKEYVDFAGG IAVTALGHCH PALVNALKTQ GETLWHISNV FTNEPALRLG RKLIEATFAE RVVFMNSGTE ANETAFKLAR HYACVRHSPF KTKIIAFHNA FHGRSLFTVS VGGQPKYSDG FGPKPADIIH VPFNDLHAVK AVMDDHTCAV VVEPIQGEGG VTAATPEFLQ GLRELCDQHQ ALLVFDEVQC GMGRTGDLFA YMHYGVTPDI LTSAKALGGG FPISAMLTTA EIASAFHPGS HGSTYGGNPL ACAVAGAAFD IINTPEVLEG IQAKRQRFVD HLQKIDQQYD VFSDIRGMGL LIGAELKPQY KGRARDFLYA GAEAGVMVLN AGPDVMRFAP SLVVEDADID EGMQRFAHAV AKVVGA // ID PLK_GIAIC Reviewed; 678 AA. AC A8BPK8; DT 24-JAN-2024, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 27-NOV-2024, entry version 97. DE RecName: Full=Serine/threonine-protein kinase PLK {ECO:0000255|RuleBase:RU361162, ECO:0000303|PubMed:33789729}; DE EC=2.7.11.21 {ECO:0000255|RuleBase:RU361162, ECO:0000269|PubMed:33789729}; DE AltName: Full=GlPLK {ECO:0000303|PubMed:33789729, ECO:0000303|PubMed:35772734}; DE AltName: Full=Polo-like kinase {ECO:0000255|RuleBase:RU361162, ECO:0000303|PubMed:33789729, ECO:0000303|PubMed:35772734}; DE Short=PLK {ECO:0000303|PubMed:33789729, ECO:0000303|PubMed:35772734}; GN Name=plk {ECO:0000303|PubMed:35772734}; GN ORFNames=GL50803_00104150 {ECO:0000312|EMBL:KAE8303276.1}, GN GL50803_104150 {ECO:0000312|EMBL:EDO78102.1}; OS Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia). OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia. OX NCBI_TaxID=184922 {ECO:0000312|EMBL:EDO78102.1}; RN [1] {ECO:0000312|EMBL:EDO78102.1, ECO:0000312|Proteomes:UP000001548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 50803 / WB clone C6 {ECO:0000312|Proteomes:UP000001548}; RX PubMed=17901334; DOI=10.1126/science.1143837; RA Morrison H.G., McArthur A.G., Gillin F.D., Aley S.B., Adam R.D., RA Olsen G.J., Best A.A., Cande W.Z., Chen F., Cipriano M.J., Davids B.J., RA Dawson S.C., Elmendorf H.G., Hehl A.B., Holder M.E., Huse S.M., Kim U.U., RA Lasek-Nesselquist E., Manning G., Nigam A., Nixon J.E.J., Palm D., RA Passamaneck N.E., Prabhu A., Reich C.I., Reiner D.S., Samuelson J., RA Svard S.G., Sogin M.L.; RT "Genomic minimalism in the early diverging intestinal parasite Giardia RT lamblia."; RL Science 317:1921-1926(2007). RN [2] {ECO:0000312|EMBL:KAE8303276.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 50803 / WB clone C6 {ECO:0000312|EMBL:KAE8303276.1}; RA Xu F., Jex A., Svard S.G.; RT "New Giardia intestinalis WB genome in near-complete chromosomes."; RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases. RN [3] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, RP DEVELOPMENTAL STAGE, PTM, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT THR-179 RP AND THR-183, AND MUTAGENESIS OF 1-MET--ASP-431; LYS-51; THR-179; THR-183 RP AND 432-PRO--GLU-678. RC STRAIN=ATCC 30957 / WB {ECO:0000303|PubMed:33789729}; RX PubMed=33789729; DOI=10.1186/s13071-021-04687-5; RA Park E.A., Kim J., Shin M.Y., Park S.J.; RT "A polo-like kinase modulates cytokinesis and flagella biogenesis in RT Giardia lamblia."; RL Parasit. Vectors 14:182-182(2021). RN [4] RP FUNCTION, INTERACTION WITH KIN-13, SUBCELLULAR LOCATION, RP AUTOPHOSPHORYLATION, AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 30957 / WB {ECO:0000303|PubMed:35772734}; RX PubMed=35772734; DOI=10.3347/kjp.2022.60.3.163; RA Park E.A., Kim J., Shin M.Y., Park S.J.; RT "Kinesin-13, a Motor Protein, is Regulated by Polo-like Kinase in Giardia RT lamblia."; RL Korean J. Parasitol. 60:163-172(2022). CC -!- FUNCTION: Involved in cell cycle (PubMed:33789729, PubMed:35772734). CC Involved in cell division (PubMed:33789729). Involved in cytokinesis CC (PubMed:33789729). Involved in flagella biogenesis and in regulation of CC flagella length in interphase (PubMed:33789729, PubMed:35772734). CC Involved in formation of median bodies during interphase CC (PubMed:35772734). Phosphorylates Kin-13 in vitro (PubMed:35772734). CC Likely regulates microtubule (MT) depolymerizing activity of Kin-13 CC (PubMed:35772734). {ECO:0000269|PubMed:33789729, CC ECO:0000269|PubMed:35772734}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.21; CC Evidence={ECO:0000255|RuleBase:RU361162, CC ECO:0000269|PubMed:33789729}; CC -!- ACTIVITY REGULATION: Inhibited by GW843286X (GW), an ATP-competitive CC inhibitor. Inhibition leads to reduced growth, increased number of CC cells with more than four nuclei, increased number of cells with CC condensed nuclei, cell cycle arrest at G2/M or G1/S phase depending on CC the treatment time with GW, and increased length of membrane-bound CC portions of the caudal and anterior flagella. CC {ECO:0000269|PubMed:33789729}. CC -!- SUBUNIT: Interacts with Kin-13. {ECO:0000269|PubMed:35772734}. CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum CC {ECO:0000269|PubMed:33789729, ECO:0000269|PubMed:35772734}. Cytoplasm, CC cytoskeleton, flagellum basal body {ECO:0000269|PubMed:33789729, CC ECO:0000269|PubMed:35772734}. Cytoplasm, cytoskeleton, flagellum CC axoneme {ECO:0000269|PubMed:33789729, ECO:0000269|PubMed:35772734}. CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:33789729, CC ECO:0000269|PubMed:35772734}. Cytoplasm, cytoskeleton, spindle CC {ECO:0000269|PubMed:33789729}. Membrane {ECO:0000269|PubMed:33789729}. CC Note=Found in both the membrane and the cytoplasmic fractions in CC interphase, G1/S and G2/M phases of the cell cycle (PubMed:33789729). CC Localizes to basal bodies, flagella, axonemes, adhesive disk and median CC bodies of trophozoites in interphase (PubMed:33789729). Remains CC localization at the basal bodies in metaphase, anaphase, telophase and CC cytokinesis (PubMed:33789729). Localizes also to mitotic spindles and CC axonemes in anaphase (PubMed:33789729). Colocalizes with microtubules CC (MTs) in the basal bodies, flagella, axonemes and median bodies in CC interphase and anaphase (PubMed:33789729). Colocalizes with MTs in the CC mitotic spindles present between two separated groups of basal bodies CC in anaphase (PubMed:33789729). Colocalizes with centrin in interphase CC as well as during cell division (PubMed:33789729). Phosphorylated form CC localizes to basal bodies and distinctly to the cytoplasmic portion of CC anterior flagella, median bodies, and flagella tips in interphase cells CC (PubMed:33789729, PubMed:35772734). Phosphorylated form localizes to CC basal bodies and mitotic spindles in dividing cells (PubMed:33789729). CC {ECO:0000269|PubMed:33789729, ECO:0000269|PubMed:35772734}. CC -!- DEVELOPMENTAL STAGE: Increased expression in interphase and G2/M phase CC compared to G1/S phase (at protein level). Phosphorylated form CC increases during the G2/M phase. Increased transcriptional expression CC in G2/M phase compared to G1/S phase. {ECO:0000269|PubMed:33789729}. CC -!- PTM: Autophosphorylated (PubMed:33789729, PubMed:35772734). CC Autophosphorylation is critical for its function in cell growth, CC cytokinesis and formation of flagella (PubMed:33789729). CC {ECO:0000269|PubMed:33789729, ECO:0000269|PubMed:35772734}. CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown results in increased number CC of cells with more than four nuclei, increased number of cells with CC condensed nuclei, time-dependent cell cycle arrest at G2/M or G1/S CC phase, and increased length of membrane-bound portions of the caudal, CC anterior and ventral flagella (PubMed:33789729). Simultaneous CC morpholino knockdown of both PLK and Kin-13 in interphase cells results CC in increased length of the caudal and anterior flagella, and to a CC lesser extent ventral flagella, and reduced volume of the median body CC (PubMed:35772734). {ECO:0000269|PubMed:33789729, CC ECO:0000269|PubMed:35772734}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. CDC5/Polo subfamily. {ECO:0000255|RuleBase:RU361162}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AACB02000030; EDO78102.1; -; Genomic_DNA. DR EMBL; AACB03000003; KAE8303276.1; -; Genomic_DNA. DR RefSeq; XP_001705776.1; XM_001705724.1. DR AlphaFoldDB; A8BPK8; -. DR SMR; A8BPK8; -. DR STRING; 184922.A8BPK8; -. DR iPTMnet; A8BPK8; -. DR EnsemblProtists; EDO78102; EDO78102; GL50803_104150. DR GeneID; 5698661; -. DR KEGG; gla:GL50803_00104150; -. DR VEuPathDB; GiardiaDB:GL50803_104150; -. DR HOGENOM; CLU_000288_46_1_1; -. DR InParanoid; A8BPK8; -. DR OMA; QRRRTIC; -. DR Proteomes; UP000001548; Chromosome 3. DR GO; GO:0005930; C:axoneme; IDA:UniProtKB. DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB. DR GO; GO:0097542; C:ciliary tip; IDA:UniProtKB. DR GO; GO:1902671; C:left anterior basal body; IDA:UniProtKB. DR GO; GO:0097554; C:left anterior flagellum; IDA:UniProtKB. DR GO; GO:1902677; C:left caudal basal body; IDA:UniProtKB. DR GO; GO:0097560; C:left caudal flagellum; IDA:UniProtKB. DR GO; GO:1902673; C:left posteriolateral basal body; IDA:UniProtKB. DR GO; GO:0097556; C:left posteriolateral flagellum; IDA:UniProtKB. DR GO; GO:1902675; C:left ventral basal body; IDA:UniProtKB. DR GO; GO:0097558; C:left ventral flagellum; IDA:UniProtKB. DR GO; GO:0097568; C:median body; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:1902672; C:right anterior basal body; IDA:UniProtKB. DR GO; GO:0097555; C:right anterior flagellum; IDA:UniProtKB. DR GO; GO:1902678; C:right caudal basal body; IDA:UniProtKB. DR GO; GO:0097561; C:right caudal flagellum; IDA:UniProtKB. DR GO; GO:1902674; C:right posteriolateral basal body; IDA:UniProtKB. DR GO; GO:0097557; C:right posteriolateral flagellum; IDA:UniProtKB. DR GO; GO:1902676; C:right ventral basal body; IDA:UniProtKB. DR GO; GO:0097559; C:right ventral flagellum; IDA:UniProtKB. DR GO; GO:0097597; C:ventral disc; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0000278; P:mitotic cell cycle; IEP:UniProtKB. DR GO; GO:1902410; P:mitotic cytokinetic process; IMP:UniProtKB. DR GO; GO:0140014; P:mitotic nuclear division; IMP:UniProtKB. DR GO; GO:1905504; P:negative regulation of motile cilium assembly; IMP:UniProtKB. DR GO; GO:1901978; P:positive regulation of cell cycle checkpoint; IMP:UniProtKB. DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. DR GO; GO:0031114; P:regulation of microtubule depolymerization; IGI:UniProtKB. DR CDD; cd13118; POLO_box_1; 1. DR CDD; cd13117; POLO_box_2; 1. DR FunFam; 3.30.200.20:FF:000042; Aurora kinase A; 1. DR Gene3D; 3.30.1120.30; POLO box domain; 2. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR033701; POLO_box_1. DR InterPro; IPR033695; POLO_box_2. DR InterPro; IPR000959; POLO_box_dom. DR InterPro; IPR036947; POLO_box_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1. DR PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1. DR Pfam; PF00069; Pkinase; 2. DR Pfam; PF00659; POLO_box; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF82615; Polo-box domain; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50078; POLO_BOX; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW ATP-binding; Cell cycle; Cell division; Cell projection; Cilium; Cytoplasm; KW Cytoskeleton; Flagellum; Kinase; Membrane; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Repeat; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..678 FT /note="Serine/threonine-protein kinase PLK" FT /id="PRO_0000459117" FT DOMAIN 22..309 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 435..516 FT /note="POLO box 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154" FT DOMAIN 563..644 FT /note="POLO box 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154" FT REGION 658..678 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 145 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 28..36 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 51 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10141" FT MOD_RES 179 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:33789729" FT MOD_RES 183 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:33789729" FT MUTAGEN 1..431 FT /note="Missing: No effect on subcellular localization." FT /evidence="ECO:0000269|PubMed:33789729" FT MUTAGEN 51 FT /note="K->R: Loss of autophosphorylation. Reduced growth, FT increased number of cells with four or more nuclei, FT increased number of cells with condensed nuclei, and FT increased length of the caudal, anterior and ventral FT flagella." FT /evidence="ECO:0000269|PubMed:33789729" FT MUTAGEN 179 FT /note="T->A: Substantial decrease in autophosphorylation, FT reduced growth, increased number of cells with four or more FT nuclei, increased number of cells with condensed nuclei, FT and increased length of the caudal, anterior and ventral FT flagella; when associated with A-183." FT /evidence="ECO:0000269|PubMed:33789729" FT MUTAGEN 183 FT /note="T->A: Substantial decrease in autophosphorylation, FT reduced growth, increased number of cells with four or more FT nuclei, increased number of cells with condensed nuclei, FT and increased length of the caudal, anterior and ventral FT flagella; when associated with A-179." FT /evidence="ECO:0000269|PubMed:33789729" FT MUTAGEN 432..678 FT /note="Missing: Does not localize to mitotic spindles at FT anaphase. Colocalizes with centrin at basal bodies of the FT dividing cells, however, the basal bodies are positioned FT incorrectly." FT /evidence="ECO:0000269|PubMed:33789729" SQ SEQUENCE 678 AA; 77190 MW; D7D73687676C5688 CRC64; MSHSNAPELH PQIVDPFHNV TYRPGKLLGK GGFAYVYEFH DVNSDSSYAC KITPRSALQK KKYYDKFVTE VTIHRGLVHP NICRVLNVFK DQMNYYIILE KCNGGTLTDL IRRRKHLTET EARFFSKRIL NALWYLHDLY IIHRDIKTSN IFLMEDFDVK VGDFGLAVKC ETPEELHWTM CGTPNFLPSE VIYSHIMKRK ASGRGPDPNL DEDCVNLCHQ LLPAYSGQGH SFSADMWSFG CLVFSMIYGR PPFEAADIKT TYKRIVRCDF SFPGSISVSE DLKNFIKGLL TPDPRKRFTV KECLDHSWLN PSKYFIPESL PPRIISEPYE VPPLCSASPT RNMQMTINMA KNAGGTDGRF IAATPQAIGG TEHIPTPGTA NFYKPQNAIL TTKSAAGISR ASTAMAMQNV GSAQGVVNKY GINEAEYPQI DPPCYIMSWV DYSNRYGFAY QISNGSIGVI FNDESAAILS PNALIVDYSP SLLDAAFDRA LFEEGTTILS EKKFKLLSFF RDYLENRSIV PIPAADRPKE DEELKRVIEQ ERMNNQEIDF KRLTKGLPLP QLFLKKWKLY DDGTLCLLFN TKVFQVNFAD HSKVVVAHRS VTFMSEKREI YTYPSEYLKD DRFSFKELRR RVDRARKYYE IIKAARPVDS LAQYRYNKDS TKKSASGSST RQLGQGGE //