ID SERC_LEGPC Reviewed; 362 AA. AC A5IBR0; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 1. DT 27-MAR-2024, entry version 83. 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=LPC_0834; OS Legionella pneumophila (strain Corby). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=400673; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Corby; RA Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E., RA Steinert M., Buchrieser C., Hacker J., Heuner K.; RT "Identification and characterization of a new conjugation/ type IVA RT secretion system (trb/tra) of L. pneumophila Corby localized on a mobile RT genomic island."; RL Submitted (NOV-2006) 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: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; CP000675; ABQ54810.1; -; Genomic_DNA. DR RefSeq; WP_011946432.1; NZ_JAPMSS010000002.1. DR AlphaFoldDB; A5IBR0; -. DR SMR; A5IBR0; -. DR KEGG; lpc:LPC_0834; -. DR HOGENOM; CLU_034866_0_2_6; -. 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 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; Aminotransferase; Cytoplasm; Pyridoxal phosphate; KW Pyridoxine biosynthesis; Serine biosynthesis; Transferase. FT CHAIN 1..362 FT /note="Phosphoserine aminotransferase" FT /id="PRO_1000058215" FT BINDING 43 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT BINDING 77..78 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT BINDING 103 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT BINDING 153 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT BINDING 173 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160" FT BINDING 196 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" 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 362 AA; 40834 MW; 18D66ABE1496A1B8 CRC64; MNSRVFNFGA GPAMLPEEIL KEAQEEFLNW RNTGMSILEI GHRTPEIINL LSTAEQSLRE LLNIPKNYHV LFLGGAARAQ FAMIPMNLLQ PGDEAAYFIT GIWSKMAYHE ANLLKQAYYL SNEEKEGFVS IPDYQKWELK SNTAYVYYTP NETINGVRFP YVPKTGGVPL VADMTSCLLS EPININQYGL IFAGAQKNIA NAGLTVVIIH EDLLKNQPEP VIPTMLNYKN HAEHRSLYAT PPVFNCYLAS KMFEWIKTQG GIEGLFQRNC LKAAKLYQYL DSTDFYLTPV SKEARSIMNI CFSLCYPDLE QKFLYMANER GLKALKGHRF AGGLRASLYN AMPMAGVDAL IEFLSEFAKE NG //