(data stored in SCRATCH zone)

SWISSPROT: B5RUD7_DEBHA

ID   B5RUD7_DEBHA            Unreviewed;       569 AA.
AC   B5RUD7;
DT   04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 1.
DT   10-APR-2019, entry version 65.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=DEHA2F10450g {ECO:0000313|EMBL:CAR66315.1};
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:CAR66315.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAR66315.1, 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=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC         Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC         Evidence={ECO:0000256|RuleBase:RU361171};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; CR382138; CAR66315.1; -; Genomic_DNA.
DR   RefSeq; XP_002770790.1; XM_002770744.1.
DR   STRING; 4959.XP_002770790.1; -.
DR   EnsemblFungi; CAR66315; CAR66315; DEHA2F10450g.
DR   GeneID; 8998936; -.
DR   KEGG; dha:DEHA2F10450g; -.
DR   HOGENOM; HOG000070228; -.
DR   InParanoid; B5RUD7; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; 521159at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR   GO; GO:0006538; P:glutamate catabolic process; IEA:EnsemblFungi.
DR   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
DR   PRODOM; B5RUD7.
DR   SWISS-2DPAGE; B5RUD7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT   MOD_RES     299    299       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   569 AA;  64257 MW;  C998EBCFDB851E55 CRC64;
     MTLSKHINAE DLESKLLKQT KKTVLDNHEE YIFKYSANAT VPKYEIPEKS SNSELVYKYI
     SEELSLDGIP TLNLASFVNT NIDDIPLRLA SENITKNLAD NDEYPSLIDI QGRCVTILSN
     LWNAPSTTDK ESGKKVINSI GSATTGSSEA IMMAGLAMKK SWQARQKANG KSIAEPNILM
     ASCAQVALEK FARYFDVENR IIHINEKSGH LIDTTKIKEN IDENTIGIFV ILGSTFTGAF
     EPVEEISKLL DEVEKERGID VKIHVDGASG GFVAPFVYPH LKWDFSIDRV ISINTSGHKF
     GLTSAGLGWI IWKDNKYLPD DVRFKLDYLG GVEETFTFNF SRPGFPVLFQ YYNFLTLGRE
     GYTKIFNSCI QNARLLSNFL EESGYFECLS VIHKGIDKER QAKIFTREHN DSSKHSKKAV
     VNEEYEPGLP VVAFRFSKEI REKYPDIPQS ILSLLLRNKG YIIPNYKLSP DEQDIEILRV
     VVRDTLGLNL LDKLMNEIVS TIELLINATD TITNLSTKEQ SSEKNEMIYS MLLSIASNGG
     EDLKEIKQQI LKDNNEQHRK HAKSYRGTC
//

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