ID I2GKJ8_9BACT Unreviewed; 358 AA.
AC I2GKJ8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
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};
GN ORFNames=BN8_03589 {ECO:0000313|EMBL:CCH54424.1};
OS Fibrisoma limi BUZ 3.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrisoma.
OX NCBI_TaxID=1185876 {ECO:0000313|EMBL:CCH54424.1, ECO:0000313|Proteomes:UP000009309};
RN [1] {ECO:0000313|EMBL:CCH54424.1, ECO:0000313|Proteomes:UP000009309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUZ 3T {ECO:0000313|Proteomes:UP000009309};
RX PubMed=22843583; DOI=10.1128/jb.00869-12;
RA Filippini M., Qi W., Jaenicke S., Goesmann A., Smits T.H., Bagheri H.C.;
RT "Genome Sequence of the Filamentous Bacterium Fibrisoma limi BUZ 3T.";
RL J. Bacteriol. 194:4445-4445(2012).
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 -!- 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}.
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:CCH54424.1}.
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DR EMBL; CAIT01000007; CCH54424.1; -; Genomic_DNA.
DR RefSeq; WP_009283002.1; NZ_CAIT01000007.1.
DR AlphaFoldDB; I2GKJ8; -.
DR STRING; 1185876.BN8_03589; -.
DR eggNOG; COG0075; Bacteria.
DR OrthoDB; 975012at2; -.
DR UniPathway; UPA00135; UER00197.
DR Proteomes; UP000009309; Unassembled WGS sequence.
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 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 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:CCH54424.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009309};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW Transferase {ECO:0000313|EMBL:CCH54424.1}.
FT DOMAIN 128..327
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 358 AA; 40885 MW; 0D910BE1E8F34557 CRC64;
MKNTYFTPGP AELYPTFYQH LQTALDEQIG SISHRSQKFR DIYKHTDEQL RILLDIPATH
GIFFTGSASE VWERILLNCV EHESFHLVNG SFSRKFYDYA QSLHKYAHLY EKPFGEGFDY
ADVEVPEYAE LVCVTHNETS SGVQMRPAEI HKLKRKYSKK LFCVDIVSSA PYPDLDFSII
DSAFFSVQKA FGMPAGLGVW IAGKSCLEKA ERLQRYDSMT IGAHHTLPTL WKNYQTFETP
ATPNVLAIYI LGKIAEDFNR IGIDTIRRQT EEKARMLYKF LDNHADYEPF VSEERHRSQT
VIVAKTKQPS ADVINAAKQA NMIVGSGYGK FKESQIRIAN FPATTIEQVT ALIDQLKK
//
