ID SERC_LIMF3 Reviewed; 357 AA. AC B2GBS2; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 1. DT 02-SEP-2026, entry version 86. 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}; GN OrderedLocusNames=LAF_0768; OS Limosilactobacillus fermentum (strain NBRC 3956 / LMG 18251) (Lactobacillus OS fermentum). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Limosilactobacillus. OX NCBI_TaxID=334390; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 3956 / LMG 18251; RX PubMed=18487258; DOI=10.1093/dnares/dsn009; RA Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T., RA Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T., RA Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T., RA Hattori M.; RT "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus RT fermentum reveal a genomic island for reuterin and cobalamin production."; RL DNA Res. 15:151-161(2008). 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=O-phospho-L-serine + 2-oxoglutarate = 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=4-(phosphooxy)-L-threonine + 2-oxoglutarate = (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 -!- 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; AP008937; BAG27104.1; -; Genomic_DNA. DR RefSeq; WP_012391123.1; NC_010610.1. DR AlphaFoldDB; B2GBS2; -. DR SMR; B2GBS2; -. DR KEGG; lfe:LAF_0768; -. DR eggNOG; COG1932; Bacteria. DR HOGENOM; CLU_034866_0_2_9; -. DR UniPathway; UPA00135; UER00197. DR Proteomes; UP000001697; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate transaminase 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 FunFam; 3.40.640.10:FF:000010; Phosphoserine aminotransferase; 1. DR FunFam; 3.90.1150.10:FF:000006; Phosphoserine aminotransferase; 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; NF003764; PRK05355.1; 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; Aminotransferase; Cytoplasm; Pyridoxal phosphate; KW Reference proteome; Serine biosynthesis; Transferase. FT CHAIN 1..357 FT /note="Phosphoserine aminotransferase" FT /id="PRO_1000097215" FT BINDING 41 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT BINDING 76..77 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT BINDING 102 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT BINDING 152 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT BINDING 171 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT BINDING 194 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT BINDING 235..236 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT MOD_RES 195 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" SQ SEQUENCE 357 AA; 39457 MW; 3B0251A1DD708A7D CRC64; MPTYNFAAGP ATLPRPVLEQ VQRELLDYQG SQVSILEISH RSPVFREIYQ QAKERLLQLM GLSADEYTPL FLQGGGTLQF TMVPLNLARD HHRVAYADTG HWSARAIEEA KKLPDLTVDV VTEAGPDFAH IPAVPDLPAD TYDYLHITTN NTIMGLAYQD LPQTAVLLVG DLSSNFLGQA YDFSSFDLIY AGAQKNLAPA GVTIVVVKND YLTEDHGLPS MLNYPALAKK ESALNTPPVF QIYFANLVLK WLKEQGGVQA MDELNRQKAG LVYDYLDQSK LFSNRVAPDS RSLTNIPFTT GKADLDQRFI KEAAAAGLVN LKGHRLVGGM RASLYNAMPL AGAVALRDFM HQFEQEI //