ID M1Q1P2_9CAUD Unreviewed; 363 AA.
AC M1Q1P2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=NifS-like protein {ECO:0000256|ARBA:ARBA00021783};
DE EC=2.6.1.52 {ECO:0000256|ARBA:ARBA00013030};
GN ORFNames=phiD12_007 {ECO:0000313|EMBL:AGF87601.1};
OS Streptococcus phage phiD12.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX NCBI_TaxID=1289600 {ECO:0000313|EMBL:AGF87601.1, ECO:0000313|Proteomes:UP000011851};
RN [1] {ECO:0000313|EMBL:AGF87601.1, ECO:0000313|Proteomes:UP000011851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23587535; DOI=10.1016/j.ygeno.2013.04.005;
RA Tang F., Bossers A., Harders F., Lu C., Smith H.;
RT "Comparative genomic analysis of twelve Streptococcus suis (pro)phages.";
RL Genomics 101:336-344(2013).
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 -!- 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; KC348603; AGF87601.1; -; Genomic_DNA.
DR SMR; M1Q1P2; -.
DR UniPathway; UPA00135; UER00197.
DR Proteomes; UP000011851; Genome.
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 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; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:AGF87601.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011851};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW Transferase {ECO:0000313|EMBL:AGF87601.1}.
FT DOMAIN 3..348
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 363 AA; 40290 MW; 379E32AE730B9F6C CRC64;
MTIYNFSAGP AVLPKPVLER AQAEFLDYNG SGMSVLEMSH RSKDFDDIIK GAEATLRELM
AIPDNYKVIF LQGGASLEFT MIPLNFAQGK KAYYLVGGSW GKKAYTEAVK LSKTIAFEPI
LLGSTEDITY AELPTFDKND IDPTAAYVHL TTNNTIEGTA VYDIPDTNGV PVIADMSSNI
LAARYNVEDF AMIYAGAQKN IGPAGVTVVI VREDFLNDQP MLSSMLDYRI QAENDSLYNT
PPAYSIYISK LVFEWVKEIG GVDEMEKINR EKSGLLYDYI DQSNFYTNPV RKKEERSVAN
IPFVSPSEEL DAKFVKEATA AGFKNIKGHR SVGGMRASLY NAFPRQGVVE LIEFMKKFAV
ENA
//
