ID SERC_MANSM Reviewed; 361 AA. AC Q65S80; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 26-FEB-2020, entry version 96. DE RecName: Full=Phosphoserine aminotransferase {ECO:0000255|HAMAP-Rule:MF_00160}; DE EC=2.6.1.52 {ECO:0000255|HAMAP-Rule:MF_00160}; DE AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000255|HAMAP-Rule:MF_00160}; DE Short=PSAT {ECO:0000255|HAMAP-Rule:MF_00160}; GN Name=serC {ECO:0000255|HAMAP-Rule:MF_00160}; OrderedLocusNames=MS1573; OS Mannheimia succiniciproducens (strain MBEL55E). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Basfia. OX NCBI_TaxID=221988; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MBEL55E; RX PubMed=15378067; DOI=10.1038/nbt1010; RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H., RA Jeong H., Hur C.G., Kim J.J.; RT "The genome sequence of the capnophilic rumen bacterium Mannheimia RT succiniciproducens."; RL Nat. Biotechnol. 22:1275-1281(2004). CC -!- FUNCTION: Catalyzes the reversible conversion of 3- CC phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- CC phosphonooxybutanoate to phosphohydroxythreonine. {ECO:0000255|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:0000255|HAMAP-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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00160}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00160}; CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00160}. CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5. CC {ECO:0000255|HAMAP-Rule:MF_00160}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00160}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00160}. CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent CC aminotransferase family. SerC subfamily. {ECO:0000255|HAMAP- CC 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; AE016827; AAU38180.1; -; Genomic_DNA. DR RefSeq; WP_011200745.1; NC_006300.1. DR SMR; Q65S80; -. DR STRING; 221988.MS1573; -. DR EnsemblBacteria; AAU38180; AAU38180; MS1573. DR KEGG; msu:MS1573; -. DR eggNOG; ENOG4107QM1; Bacteria. DR eggNOG; COG1932; LUCA. DR HOGENOM; CLU_034866_0_2_6; -. DR KO; K00831; -. DR OMA; GAQKNMG; -. DR OrthoDB; 996960at2; -. DR BioCyc; MSUC221988:MS_RS07185-MONOMER; -. DR UniPathway; UPA00135; UER00197. DR UniPathway; UPA00244; UER00311. DR Proteomes; UP000000607; Chromosome. 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; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_00160; SerC_aminotrans_5; 1. DR InterPro; IPR000192; Aminotrans_V_dom. DR InterPro; IPR022278; Pser_aminoTfrase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF000525; SerC; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR01364; serC_1; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aminotransferase; Cytoplasm; Pyridoxal phosphate; KW Pyridoxine biosynthesis; Serine biosynthesis; Transferase. FT CHAIN 1..361 FT /note="Phosphoserine aminotransferase" FT /id="PRO_0000150186" FT REGION 76..77 FT /note="Pyridoxal phosphate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT REGION 238..239 FT /note="Pyridoxal phosphate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT BINDING 42 FT /note="L-glutamate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT BINDING 102 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT BINDING 153 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT BINDING 173 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT BINDING 196 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT MOD_RES 197 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" SQ SEQUENCE 361 AA; 39988 MW; C13EF5C92426CCFE CRC64; MSNVFNFSAG PAMMPPAVLK KAQEELLNWQ GQGTSVMEVS HRGKYFMELI TQADKDFREL YNIPENYKIL FLQGGARGQF AAIPMNLANN KGKALYLNTG HWSATAAKEA RNFTEVDELN ITEQIDGLTR VNRLDFSDIA EQYDYVHYCP NETITGVEIN EIPNVGNAVL VADMSSNIMA RKLDISKFGI IYAGAQKNLG PAGIVIVIVR EDLIGHARKA TPSIWNYEVQ ANADSMINTP PTFAWYLCSL VFKDLLANGG IDTVEKRNAQ KAALLYDYLD QTVFYHNTIA KENRSVMNVT FTTGDDQLNA KFVAQATEAG LQALKGHKVF GGMRASIYNA MPVEGVEALI AFMKKFEAEN A //