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Database: UniProt/TrEMBL
Entry: C5P207_COCP7
LinkDB: C5P207_COCP7
Original site: C5P207_COCP7 
ID   C5P207_COCP7            Unreviewed;       517 AA.
AC   C5P207;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   20-DEC-2017, entry version 50.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=CPC735_036160 {ECO:0000313|EMBL:EER28910.1};
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Coccidioides.
OX   NCBI_TaxID=222929 {ECO:0000313|EMBL:EER28910.1, ECO:0000313|Proteomes:UP000009084};
RN   [1] {ECO:0000313|EMBL:EER28910.1, ECO:0000313|Proteomes:UP000009084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735 {ECO:0000313|Proteomes:UP000009084};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J.,
RA   Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E.,
RA   Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M.,
RA   Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N., Orbach M.J.,
RA   Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens
RT   Coccidioides and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EER28910.1}.
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DR   EMBL; ACFW01000012; EER28910.1; -; Genomic_DNA.
DR   RefSeq; XP_003071055.1; XM_003071009.1.
DR   UniGene; Cpo.5790; -.
DR   ProteinModelPortal; C5P207; -.
DR   STRING; 222929.XP_003071055.1; -.
DR   EnsemblFungi; EER28910; EER28910; CPC735_036160.
DR   GeneID; 9696550; -.
DR   KEGG; cpw:CPC735_036160; -.
DR   EuPathDB; FungiDB:CPC735_036160; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000009084; Unassembled 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:0006536; P:glutamate metabolic process; IEA:InterPro.
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; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000009084};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:EER28910.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     296    296       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   517 AA;  58867 MW;  F89190FE7FAEFC20 CRC64;
     MVHLAAVRKD SEVLPLRMVK RVDTIPLEEP QEHDFFSSVY GSRFAAEDLP THEMPEKEMP
     REVAYRMIKD ELSLDGNPML NLASFVTTYM EEEAERLMAE SFSKNFIDYE EYPQSAEIQN
     RCVNMIARLF NAPASDESDH AMGTSCVGSS EAIMLGTLAM KKRWQNKRKA EGKDYSRPNI
     IMSSAVQVCW EKAARYFDVE EKFVYCTSER YVIDPEEAIS MVDENTIGIC AILGTTYTGQ
     YEDIKALNDI MIEKVIDCPI HVDAASGGFV APFVNPNLEW DFRLEKVVSI NVSGHKYGLV
     YPGVGWVVWR SPEYLPKELV FNINYLGANQ ASFTLNFSKG ASQVIGQYYQ MIRLGKRGYR
     SIMVNLTRTA DYLASALRQL GFIIMSDGKG HGLPLVAFRL NPDDENVMYD EFALAHQLRE
     RGWVVPAYTM APHSEKLKLM RIVVREDFSK SRCDNLVNDI KLALQQLGDM DKRTLERFQQ
     HIRRHVTNSG SATHNHPQYQ DEDHSLQGKT GKTHAIC
//
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