ID O88149_NEIME Unreviewed; 150 AA.
AC O88149;
DT 01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1998, sequence version 1.
DT 24-JAN-2024, entry version 99.
DE RecName: Full=Phosphoserine aminotransferase {ECO:0000256|ARBA:ARBA00021164};
DE EC=2.6.1.52 {ECO:0000256|ARBA:ARBA00013030};
DE AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000256|ARBA:ARBA00031421};
DE AltName: Full=Putative 8-amino-7-oxononanoate synthase {ECO:0000256|ARBA:ARBA00021531};
DE Flags: Fragment;
GN Name=serC {ECO:0000313|EMBL:AAC08693.1};
OS Neisseria meningitidis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=487 {ECO:0000313|EMBL:AAC08693.1};
RN [1] {ECO:0000313|EMBL:AAC08693.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9501229; DOI=10.1073/pnas.95.6.3140;
RA Maiden M.C., Bygraves J.A., Feil E., Morelli G., Russell J.E., Urwin R.,
RA Zhang Q., Zhou J., Zurth K., Caugant D.A., Feavers I.M., Achtman M.,
RA Spratt B.G.;
RT "Multilocus sequence typing: a portable approach to the identification of
RT clones within populations of pathogenic microorganisms.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:3140-3145(1998).
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};
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};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004504};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 2/3. {ECO:0000256|ARBA:ARBA00005099}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily.
CC {ECO:0000256|ARBA:ARBA00006904}.
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DR EMBL; AF037957; AAC08670.1; -; Genomic_DNA.
DR EMBL; AF037973; AAC08686.1; -; Genomic_DNA.
DR EMBL; AF037980; AAC08693.1; -; Genomic_DNA.
DR AlphaFoldDB; O88149; -.
DR UniPathway; UPA00135; UER00197.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
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 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 PANTHER; PTHR43247; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43247:SF1; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR Pfam; PF00266; Aminotran_5; 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 {ECO:0000256|ARBA:ARBA00022605};
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:AAC08693.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW Transferase {ECO:0000313|EMBL:AAC08693.1}.
FT DOMAIN 2..138
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAC08693.1"
FT NON_TER 150
FT /evidence="ECO:0000313|EMBL:AAC08693.1"
SQ SEQUENCE 150 AA; 16959 MW; 8B592F29A5AE6DC7 CRC64;
LSREFDVADY GLIYAGAQKN IGPAGVTVVI VREDLLERCP NDIPDVFNYR SHINRDGMYN
TPSTYAIYMS GLVFRWLQAQ GGVKKIEAVN RLKAQTLYET IDGSGGFYIN RIRPNARSKM
NVVFQTGDEE LDRRFVLEAE LQGLCLLKGY
//
