ID A0A0H5CTJ5_9PSEU Unreviewed; 378 AA. AC A0A0H5CTJ5; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 05-OCT-2016, entry version 10. 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}; GN Name=serC {ECO:0000256|HAMAP-Rule:MF_00160}; OS Alloactinosynnema sp. L-07. OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae. OX NCBI_TaxID=1653480 {ECO:0000313|EMBL:CRK61329.1, ECO:0000313|Proteomes:UP000076116}; RN [1] {ECO:0000313|EMBL:CRK61329.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=L-07 {ECO:0000313|EMBL:CRK61329.1}; RA Ramaraj Thiru; RL Submitted (MAY-2015) 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. CC {ECO:0000256|HAMAP-Rule:MF_00160, ECO:0000256|SAAS:SAAS00019536}. CC -!- CATALYTIC ACTIVITY: 4-phosphonooxy-L-threonine + 2-oxoglutarate = CC (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. CC {ECO:0000256|HAMAP-Rule:MF_00160, ECO:0000256|SAAS:SAAS00182458}. CC -!- CATALYTIC ACTIVITY: O-phospho-L-serine + 2-oxoglutarate = 3- CC phosphonooxypyruvate + L-glutamate. {ECO:0000256|HAMAP- CC Rule:MF_00160, ECO:0000256|SAAS:SAAS00182418}. 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 CC from 3-phospho-D-glycerate: step 2/3. {ECO:0000256|HAMAP- CC Rule:MF_00160, ECO:0000256|SAAS:SAAS00182464}. CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate CC biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4- CC phosphate: step 3/5. {ECO:0000256|HAMAP-Rule:MF_00160}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00160, CC ECO:0000256|SAAS:SAAS00148734}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160, CC ECO:0000256|SAAS:SAAS00019491}. CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent CC aminotransferase family. SerC subfamily. {ECO:0000256|HAMAP- CC Rule:MF_00160, ECO:0000256|SAAS:SAAS00542307}. 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; LN850107; CRK61329.1; -; Genomic_DNA. DR UniPathway; UPA00135; UER00197. DR UniPathway; UPA00244; UER00311. DR Proteomes; UP000076116; Chromosome i. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-HAMAP. 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; IPR006272; Pser_aminoTfrase_mycobac. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF000525; SerC; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR01366; serC_3; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160, KW ECO:0000256|SAAS:SAAS00425538}; KW Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160, KW ECO:0000256|SAAS:SAAS00425559, ECO:0000313|EMBL:CRK61329.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000076116}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160, KW ECO:0000256|SAAS:SAAS00425508}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00160, KW ECO:0000256|SAAS:SAAS00425647}; KW Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160}; KW Reference proteome {ECO:0000313|Proteomes:UP000076116}; KW Serine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160, KW ECO:0000256|SAAS:SAAS00425644}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00160, KW ECO:0000256|SAAS:SAAS00425627, ECO:0000313|EMBL:CRK61329.1}. FT DOMAIN 41 336 Aminotran_5. {ECO:0000259|Pfam:PF00266}. FT REGION 85 86 Pyridoxal phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00160}. FT REGION 252 253 Pyridoxal phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00160}. FT BINDING 51 51 L-glutamate. {ECO:0000256|HAMAP-Rule: FT MF_00160}. FT BINDING 109 109 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00160}. FT BINDING 155 155 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00160}. FT BINDING 177 177 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00160}. FT BINDING 200 200 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00160}. FT MOD_RES 201 201 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|HAMAP-Rule:MF_00160}. SQ SEQUENCE 378 AA; 40060 MW; A6282419B91F2477 CRC64; MTQTADPSTL VLPADLQPSD GRFGCGPSKV RPEQVAALAS EGAKLLGTSH RQKPVKSLVG RVRTGLRDLF SIPDDYEVVL GNGGATAFWD IAAFGLVRER SQHFTNGEFS AKFAAATKGA PFLADPIVVK AEPGTAPEIV YAEGADLVGW AQNETSTGVQ MPVARPAGSG DALIAVDATS GAGGLPVNAA DADVYYFGPQ KCFAADGGLW LALMSPAALA RAAEIGASDR WIPEFLSLTT AIDNSAKDQT YNTPAISTLF LLAEQIDWML ANGGLDWTVA RTKDSSSRLY SWAEERDFTS PYVAEPAHRS QVVGTIDFAD SIDAATVAKV LRANGIVDVE PYRKLGRNQL RVAMFPAIEP DDITTLTGAI DWVVEQLG //