(data stored in ACNUC7421 zone)

SWISSPROT: D4YXD7_SPHJU

ID   D4YXD7_SPHJU            Unreviewed;       387 AA.
AC   D4YXD7;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=Phosphoserine transaminase {ECO:0000256|SAAS:SAAS00347504};
DE            EC=2.6.1.52 {ECO:0000256|SAAS:SAAS00347504};
GN   Name=serC {ECO:0000313|EMBL:BAI95019.1};
GN   OrderedLocusNames=SJA_C1-01850 {ECO:0000313|EMBL:BAI95019.1};
OS   Sphingobium japonicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26
OS   / NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95019.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95019.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S
RC   {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC       phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC       phosphonooxybutanoate to phosphohydroxythreonine.
CC       {ECO:0000256|SAAS:SAAS00347519}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-
CC         hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate;
CC         Xref=Rhea:RHEA:16573, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58452, ChEBI:CHEBI:58538; EC=2.6.1.52;
CC         Evidence={ECO:0000256|SAAS:SAAS01118610};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + O-phospho-L-serine = 3-
CC         phosphooxypyruvate + L-glutamate; Xref=Rhea:RHEA:14329,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:18110, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57524; EC=2.6.1.52;
CC         Evidence={ECO:0000256|SAAS:SAAS01118608};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|SAAS:SAAS00608121};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 2/3.
CC       {ECO:0000256|SAAS:SAAS00182464}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|SAAS:SAAS00347516}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00019491}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. SerC subfamily.
CC       {ECO:0000256|SAAS:SAAS00542307}.
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DR   EMBL; AP010803; BAI95019.1; -; Genomic_DNA.
DR   RefSeq; WP_013038827.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-01850; -.
DR   EnsemblBacteria; BAI95019; BAI95019; SJA_C1-01850.
DR   GeneID; 29271891; -.
DR   KEGG; sjp:SJA_C1-01850; -.
DR   eggNOG; ENOG4107R1T; Bacteria.
DR   eggNOG; COG1932; LUCA.
DR   HOGENOM; HOG000139599; -.
DR   KO; K00831; -.
DR   OMA; ETDVYYF; -.
DR   UniPathway; UPA00135; UER00197.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR022278; Pser_aminoTfrase.
DR   InterPro; IPR006271; Pser_aminoTfrase_methanosarc.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000525; SerC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01365; serC_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YXD7.
DR   SWISS-2DPAGE; D4YXD7.
KW   Amino-acid biosynthesis {ECO:0000256|SAAS:SAAS00182425};
KW   Aminotransferase {ECO:0000256|SAAS:SAAS00182445,
KW   ECO:0000313|EMBL:BAI95019.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00425508};
KW   Pyridoxal phosphate {ECO:0000256|SAAS:SAAS00182424};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Serine biosynthesis {ECO:0000256|SAAS:SAAS00182451};
KW   Transferase {ECO:0000256|SAAS:SAAS00182455,
KW   ECO:0000313|EMBL:BAI95019.1}.
FT   DOMAIN      118    343       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
SQ   SEQUENCE   387 AA;  41431 MW;  98499BF0D5ABD8E2 CRC64;
     MTDTTAADAT IAPAAKPATK PARPYFSSGP CAKPPGWSAD KLSAESLGRS HRAKIGKTRL
     AYCIDLMREL LNLPDTHRIG IVPGSDTGAF EMAMWTMLGA RPVTTLAWES FGEGWVTDAA
     KQLKLDPTII RADYGQLPDL NGVNFAHDVL FTWNGTTSGV RVPNADWIPS TREGLTFADA
     TSAVFAYEID WTKIDVATFS WQKVLGGEGG HGVLILGPRA VERLETHTPA WPLPKVFRLM
     AKGKLAEGVF KGETINTPSM LAVEDAIFAL EWGKSLGGLS GLIARSNANA AALNKIVEER
     DWLGHLAADP ASRSTTSVCL KVEGADEAFI KSFAALLEKE GAAYDVAGYR DAPAGLRIWC
     GATVETADIE ALGPWLDWAY AQTKAAA
//

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