GenomeNet

Database: UniProt
Entry: X5DWK4_9CORY
LinkDB: X5DWK4_9CORY
Original site: X5DWK4_9CORY 
ID   X5DWK4_9CORY            Unreviewed;       377 AA.
AC   X5DWK4;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
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   Name=serC {ECO:0000313|EMBL:AHW64997.1};
GN   ORFNames=CGLY_12785 {ECO:0000313|EMBL:AHW64997.1};
OS   Corynebacterium glyciniphilum AJ 3170.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1404245 {ECO:0000313|EMBL:AHW64997.1, ECO:0000313|Proteomes:UP000023703};
RN   [1] {ECO:0000313|EMBL:AHW64997.1, ECO:0000313|Proteomes:UP000023703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AJ 3170 {ECO:0000313|EMBL:AHW64997.1};
RX   PubMed=25323597; DOI=10.1099/ijs.0.065102-0;
RA   Al-Dilaimi A., Bednarz H., Lomker A., Niehaus K., Kalinowski J.,
RA   Ruckert C.;
RT   "Revisiting Corynebacterium glyciniphilum (ex Kubota et al., 1972) sp.
RT   nov., nom. rev., isolated from putrefied banana.";
RL   Int. J. Syst. Evol. Microbiol. 65:177-182(2015).
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   ---------------------------------------------------------------------------
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; CP006842; AHW64997.1; -; Genomic_DNA.
DR   RefSeq; WP_038550013.1; NZ_CP006842.1.
DR   AlphaFoldDB; X5DWK4; -.
DR   STRING; 1404245.CGLY_12785; -.
DR   KEGG; cgy:CGLY_12785; -.
DR   eggNOG; COG1932; Bacteria.
DR   HOGENOM; CLU_061974_0_0_11; -.
DR   OrthoDB; 975012at2; -.
DR   UniPathway; UPA00135; UER00197.
DR   Proteomes; UP000023703; Chromosome.
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; IPR006272; Pser_aminoTfrase_mycobac.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01366; serC_3; 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:AHW64997.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023703};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW   Transferase {ECO:0000313|EMBL:AHW64997.1}.
FT   DOMAIN          142..332
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   377 AA;  40213 MW;  F64046698F4FF6FA CRC64;
     MSDQFPTLPE NLLPADGRFG CGPSKVRQDQ IDAIVSGSRD IIGTSHRQPA VKNLVGSVRE
     GLSTLFNLPE GYEIITSLGG ATAFWDSASF GLIRNKSAHL TYGEFSGKFA SVSKKAPWLE
     APEVVASEPG TAPSPGQLDG VDADLVGWAH NETSTGAMVD VTRPATDALV AIDATSGAGG
     LPVDIAETDV YYFSPQKCFA SDGGLWFAAF SPSALERVEE IAATDRYIPA FLDLKTAVDN
     SRKNQTYNTP AVGTLLMMDA QVKWMNANGG LDGMVARTSE SSSTLYNWAE SRPETSPFVA
     DPSSRSLVVG TIDFEESVDA DVIAKTLRAN GVLDTEPYRK LGRNQLRIGM FPAIDPEDVR
     TLTGAIDHIL DSGIATR
//
DBGET integrated database retrieval system