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 06-MAR-2007, entry version 21. DE Phosphoserine aminotransferase (EC 2.6.1.52) (PSAT). GN Name=serC; OrderedLocusNames=MS1573; OS Mannheimia succiniciproducens (strain MBEL55E). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Mannheimia. OX NCBI_TaxID=221988; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., RA Kim C.H., 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 -!- CATALYTIC ACTIVITY: O-phospho-L-serine + 2-oxoglutarate = 3- CC phosphonooxypyruvate + L-glutamate. CC -!- CATALYTIC ACTIVITY: 4-phosphonooxy-L-threonine + 2-oxoglutarate = CC (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine CC from 3-phospho-D-glycerate: step 2. CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate CC biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4- CC phosphate: step 3. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent CC aminotransferase family. 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 GenomeReviews; AE016827_GR; MS1573. DR KEGG; msu:MS1573; -. DR GO; GO:0004648; F:phosphoserine transaminase activity; IEA:HAMAP. DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:HAMAP. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00160; -; 1. DR InterPro; IPR000192; Aminotrans_V. DR InterPro; IPR003248; Pser_amintransf. DR Pfam; PF00266; Aminotran_5; 1. DR ProDom; PD001544; Pser_amintransf; 1. DR TIGRFAMs; TIGR01364; serC_1; 1. DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; FALSE_NEG. KW Amino-acid biosynthesis; Aminotransferase; Complete proteome; KW Pyridoxal phosphate; Pyridoxine biosynthesis; Serine biosynthesis; KW Transferase. FT CHAIN 1 361 Phosphoserine aminotransferase. FT /FTId=PRO_0000150186. FT BINDING 197 197 Pyridoxal phosphate (covalent) (By FT similarity). 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 //