(data stored in SCRATCH zone)

SWISSPROT: Q6BMW0_DEBHA

ID   Q6BMW0_DEBHA            Unreviewed;       393 AA.
AC   Q6BMW0;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 95.
DE   RecName: Full=Phosphoserine aminotransferase {ECO:0000256|RuleBase:RU004505};
DE            EC=2.6.1.52 {ECO:0000256|RuleBase:RU004505};
GN   OrderedLocusNames=DEHA2F02200g {ECO:0000313|EMBL:CAG88767.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88767.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88767.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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|RuleBase:RU004505};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU004504};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 2/3.
CC       {ECO:0000256|RuleBase:RU004505}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU004075}.
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DR   EMBL; CR382138; CAG88767.1; -; Genomic_DNA.
DR   RefSeq; XP_460460.1; XM_460460.1.
DR   STRING; 4959.XP_460460.1; -.
DR   EnsemblFungi; CAG88767; CAG88767; DEHA2F02200g.
DR   GeneID; 2903963; -.
DR   KEGG; dha:DEHA2F02200g; -.
DR   HOGENOM; HOG000088965; -.
DR   InParanoid; Q6BMW0; -.
DR   KO; K00831; -.
DR   OMA; GAQKNMG; -.
DR   OrthoDB; 1357311at2759; -.
DR   UniPathway; UPA00135; UER00197.
DR   Proteomes; UP000000599; Chromosome F.
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:0009113; P:purine nucleobase biosynthetic process; IEA:EnsemblFungi.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00160; SerC_aminotrans_5; 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; 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; TIGR01364; serC_1; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BMW0.
DR   SWISS-2DPAGE; Q6BMW0.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004505};
KW   Aminotransferase {ECO:0000256|RuleBase:RU004505};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Serine biosynthesis {ECO:0000256|RuleBase:RU004505};
KW   Transferase {ECO:0000256|RuleBase:RU004505}.
FT   DOMAIN       15    381       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
SQ   SEQUENCE   393 AA;  43316 MW;  20D19F4E97E88D68 CRC64;
     MAQERTLNRE EPHYFGAGPA LLPTSVLQEA AYDLITYGDE NIGVGEISHR SKPAIGIIDS
     TKEKLSELMN IPDTHEVFFM QGGGTTGFSS IVYNLMANYT KRTGKKGKAA YAITGSWSAK
     AAEESKRLGF ETDIVVNTKN RKYGDIPPYS EWKSIDKEST AYLYVCDNET VNGNEFQDTP
     GPNYLPEGVE LVSDMSSNIL SKEIDVSKYG LIMAGAQKNI GLAGLTIYII KKSLLEQASD
     EELNSKNIPL TPIAFHYPTV VKNNSAYNTI PIFTCHMINL VLKKLQDAGG VSAMEKTNEQ
     KAKTLYGALE NYPNFYKMPV TNRSVRSRMN VVFNLPNADL EAKFVSEAAE RKLTGLKGHR
     SVGGIRASIY NAVSLESVEL LVKFVNDFAE ANK
//

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