ID A0A5M9ZNU8_9BIFI Unreviewed; 381 AA. AC A0A5M9ZNU8; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 22-FEB-2023, entry version 13. 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 ORFNames=EMO89_08135 {ECO:0000313|EMBL:KAA8829311.1}; OS Bifidobacterium tissieri. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=1630162 {ECO:0000313|EMBL:KAA8829311.1, ECO:0000313|Proteomes:UP000412028}; RN [1] {ECO:0000313|EMBL:KAA8829311.1, ECO:0000313|Proteomes:UP000412028} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RST7 {ECO:0000313|EMBL:KAA8829311.1, RC ECO:0000313|Proteomes:UP000412028}; RX PubMed=31585749; RA Modesto M., Satti M., Watanabe K., Puglisi E., Morelli L., Huang C.-H., RA Liou J.-S., Miyashita M., Tamura T., Saito S., Mori K., Huang L., RA Sciavilla P., Sandri C., Spiezio C., Vitali F., Cavalieri D., RA Perpetuini G., Tofalo R., Bonetti A., Arita M., Mattarelli P.; RT "Characterization of Bifidobacterium species in feaces of the Egyptian RT fruit bat: Description of B. vespertilionis sp. nov. and B. rousetti sp. RT nov."; RL Syst. Appl. Microbiol. 42:126017-126017(2019). 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}; 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}. 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00160}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAA8829311.1}. 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; RZUI01000010; KAA8829311.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5M9ZNU8; -. DR OrthoDB; 975012at2; -. DR UniPathway; UPA00135; UER00197. DR UniPathway; UPA00244; UER00311. DR Proteomes; UP000412028; Unassembled WGS sequence. 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; IPR022278; Pser_aminoTfrase. DR InterPro; IPR006272; Pser_aminoTfrase_mycobac. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1. DR PANTHER; PTHR21152:SF24; SERINE--PYRUVATE AMINOTRANSFERASE; 1. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF000525; SerC; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR TIGRFAMs; TIGR01366; serC_3; 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:0000313|EMBL:KAA8829311.1}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00160}; KW Pyridoxine biosynthesis {ECO:0000256|HAMAP-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:0000313|EMBL:KAA8829311.1}. FT DOMAIN 138..345 FT /note="Aminotransferase class V" FT /evidence="ECO:0000259|Pfam:PF00266" FT BINDING 46 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160" FT BINDING 80..81 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160" FT BINDING 104 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160" FT BINDING 150 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 255..256 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 381 AA; 41350 MW; 5EE7D36AF2B5D252 CRC64; MIEPVKIPMS MLPEDGRFGC GPSKIRHKQV KALTEAGYNL LGTSHRQAPV KHVVASIREG LSDYFSIPEG WQIALGNGGA SAFWEVACAS LISRRAAFGT YGSFSGKFAT SAAKAPFLEE PVIYKAEYGS CAIPQYTDDV DAYCWAQNET STGVMAPVHR VPGSVEQGAL TLIDATSGAG GLPIDISQTD AYYFSPQKVF GSDGGLWFAI LSPDAIKRAE DVEKSAELEG ARRWVPPFLS LTQALANSRK DQTLNTPAIS TLVLMDEQVR WLNEHGGLTW AQERCAKSAD ILYTWAEKSD YATPFVSDPS LRSNVVVTID LDDSIKAAAV VAVLRDNGIV DTSGYRKLGR NQLRIGVFPS VKPSDVEALT YCIDYVVEHL Q //