GenomeNet

Database: UniProt/TrEMBL
Entry: C1H139_PARBA
LinkDB: C1H139_PARBA
Original site: C1H139_PARBA 
ID   C1H139_PARBA            Unreviewed;       552 AA.
AC   C1H139;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   05-JUL-2017, entry version 47.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=PAAG_04483 {ECO:0000313|EMBL:EEH33433.1};
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis;
OC   Paracoccidioides.
OX   NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH33433.1, ECO:0000313|Proteomes:UP000002059};
RN   [1] {ECO:0000313|EMBL:EEH33433.1, ECO:0000313|Proteomes:UP000002059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A.,
RA   Goldberg J., Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M.,
RA   Grynberg M., Gujja S., Heiman D.I., Henn M.R., Kodira C.D.,
RA   Leon-Narvaez H., Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L.,
RA   Morais F.V., Pereira M., Rodriguez-Brito S., Sakthikumar S.,
RA   Salem-Izacc S.M., Sykes S.M., Teixeira M.M., Vallejo M.C.,
RA   Walter M.E., Yandava C., Young S., Zeng Q., Zucker J., Felipe M.S.,
RA   Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G., Puccia R.,
RA   San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; KN294002; EEH33433.1; -; Genomic_DNA.
DR   RefSeq; XP_002793573.1; XM_002793527.1.
DR   STRING; 502779.XP_002793573.1; -.
DR   EnsemblFungi; EEH33433; EEH33433; PAAG_04483.
DR   GeneID; 9096738; -.
DR   KEGG; pbl:PAAG_04483; -.
DR   EuPathDB; FungiDB:PAAG_04483; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000002059; Partially assembled WGS sequence.
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   Gene3D; 3.90.1150.10; -; 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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 2.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002059};
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:UP000002059}.
FT   MOD_RES     302    302       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   552 AA;  61741 MW;  04B5413F734F4828 CRC64;
     MSLACHVDAN KLVEELRSDP ERRKSERLWT ESVSGSMIPY PTRYASREEI PRFKIPKEGA
     PAEAVRRMLR DHLDLDGIPN LNMASFVGTY MEREADELLS ENINKNLADA DEYPALMEMH
     AHCVSMLANL WNAQPGGNAI GSATTGSSEA IHLGGLAMKR RWQEKRRAAG KDISKPNIIM
     GANAQVALLK FARYFEVEPR ILDVSEKSQY RLDPELVKKN VDENTLGVFV ILGSTYTGHY
     EPVEEISNIL DEYQAKTGED VPIHVDAASG GFVAPFAFAQ AGGSKWDFLL PRVKSINTSG
     HKFGLVYAGL GWIIWRDRSY LPKDLIFELH YLGGTEETFT LNFSRPGMQV IGQYYNFIRL
     GFNGYREIME NCLANARLLS KALEKTGWFV CVSDIHRKKG NFNLGQTAEE LKELLKNVEG
     ETSADYNAGL PVVAFRLSDV FQKKYPDVKQ DSISLLLRAK QYIIPNYPLP PAVDKTEILR
     IVVRESMSAD LIDRLVADTV AITEKLMEKP VDIAALHTGS TSIARRHMAA NGERGAKGTR
     KHHPDGIHRS VC
//
DBGET integrated database retrieval system