ID A0A6M3NV70_SALET Unreviewed; 362 AA. AC A0A6M3NV70; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 08-NOV-2023, entry version 16. DE RecName: Full=Phosphoserine aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160}; DE EC=2.6.1.52 {ECO:0000256|HAMAP-Rule:MF_00160}; DE AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160}; DE Short=PSAT {ECO:0000256|HAMAP-Rule:MF_00160}; GN Name=serC {ECO:0000256|HAMAP-Rule:MF_00160, GN ECO:0000313|EMBL:QJB96923.1}; GN ORFNames=G4F93_14160 {ECO:0000313|EMBL:QJB96923.1}; OS Salmonella enterica subsp. enterica serovar Worthington. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=1160769 {ECO:0000313|EMBL:QJB96923.1}; RN [1] {ECO:0000313|EMBL:QJB96923.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=OLF-FSR1_WB_Partridge_SW-37 {ECO:0000313|EMBL:QJB96923.1}; RA Naushad S., Duceppe M.-O., Dupras A.A., Gao R., Ogunremi D.; RT "Closed genome sequences and antimicrobial resistance profile of eight wild RT bird Salmonella strains obtained with MinIon and MiSeq sequencing."; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reversible conversion of 3- CC phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- CC phosphonooxybutanoate to phosphohydroxythreonine. {ECO:0000256|HAMAP- CC Rule:MF_00160}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2- CC oxo-4-phosphooxybutanoate + L-glutamate; Xref=Rhea:RHEA:16573, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58452, CC ChEBI:CHEBI:58538; EC=2.6.1.52; CC Evidence={ECO:0000256|ARBA:ARBA00001607, ECO:0000256|HAMAP- CC Rule:MF_00160}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + CC L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52; CC Evidence={ECO:0000256|ARBA:ARBA00001871, ECO:0000256|HAMAP- CC Rule:MF_00160, ECO:0000256|RuleBase:RU004505}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00160}; CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00160}; CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from CC 3-phospho-D-glycerate: step 2/3. {ECO:0000256|ARBA:ARBA00005099, CC ECO:0000256|HAMAP-Rule:MF_00160, ECO:0000256|RuleBase:RU004505}. CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5. CC {ECO:0000256|HAMAP-Rule:MF_00160}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00160}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160}. CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent CC aminotransferase family. SerC subfamily. CC {ECO:0000256|ARBA:ARBA00006904, ECO:0000256|HAMAP-Rule:MF_00160}. 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; CP051273; QJB96923.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6M3NV70; -. DR SMR; A0A6M3NV70; -. DR UniPathway; UPA00135; UER00197. DR UniPathway; UPA00244; UER00311. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule. DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00611; PSAT_like; 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_00160; SerC_aminotrans_5; 1. DR InterPro; IPR000192; Aminotrans_V_dom. DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS. DR InterPro; IPR022278; Pser_aminoTfrase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR NCBIfam; TIGR01364; serC_1; 1. DR PANTHER; PTHR43247; PHOSPHOSERINE AMINOTRANSFERASE; 1. DR PANTHER; PTHR43247:SF1; PHOSPHOSERINE AMINOTRANSFERASE; 1. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF000525; SerC; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00160}; KW Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160, KW ECO:0000256|RuleBase:RU004505}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP- KW Rule:MF_00160}; KW Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096, ECO:0000256|HAMAP- KW Rule:MF_00160}; KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299, ECO:0000256|HAMAP- KW Rule:MF_00160}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00160, KW ECO:0000256|RuleBase:RU004505}. FT DOMAIN 4..350 FT /note="Aminotransferase class V" FT /evidence="ECO:0000259|Pfam:PF00266" FT BINDING 9 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160" FT BINDING 42 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160" FT BINDING 76..77 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160" FT BINDING 102 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160" FT BINDING 153 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160" FT BINDING 174 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160" FT BINDING 197 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160" FT BINDING 239..240 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160" FT MOD_RES 198 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160" SQ SEQUENCE 362 AA; 39832 MW; 802C026A8B4CE2C3 CRC64; MAQVFNFSSG PAMLPAEVLK LAQQELCDWH GLGTSVMEIS HRGKEFIQVA EEAEQDFRDL LNIPSNYKVL FCHGGGRGQF AGVPLNLLGD KTTADYVDAG YWAASAIKEA KKYCAPQIID AKITVDGKRA VKPMREWQLS DNAAYLHYCP NETIDGIAID ETPDFGPEVV VTADFSSTIL SAPLDVSRYG VIYAGAQKNI GPAGLTLVIV REDLLGKAHE SCPSILDYTV LNDNDSMFNT PPTFAWYLSG LVFKWLKAQG GVAAMHKINQ QKAELLYGVI DNSDFYRNDV AQANRSRMNV PFQLADNTLD KVFLEESFAA GLHALKGHRV VGGMRASIYN AMPIEGVKAL TDFMIDFERR HG //