ID   C5NZG0_COCP7            Unreviewed;       558 AA.
AC   C5NZG0;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
GN   ORFNames=CPC735_011710 {ECO:0000313|EMBL:EER29853.1};
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=222929 {ECO:0000313|EMBL:EER29853.1, ECO:0000313|Proteomes:UP000009084};
RN   [1] {ECO:0000313|EMBL:EER29853.1, 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., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, 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 EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EER29853.1}.
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DR   EMBL; ACFW01000001; EER29853.1; -; Genomic_DNA.
DR   RefSeq; XP_003071998.1; XM_003071952.1.
DR   AlphaFoldDB; C5NZG0; -.
DR   GeneID; 9697493; -.
DR   KEGG; cpw:CPC735_011710; -.
DR   VEuPathDB; FungiDB:CPC735_011710; -.
DR   HOGENOM; CLU_019582_2_3_1; -.
DR   OrthoDB; 2783360at2759; -.
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; 3.90.1150.160; -; 1.
DR   Gene3D; 4.10.280.50; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR   PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43321:SF3; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES         302
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   558 AA;  62988 MW;  07F70E2F4E555836 CRC64;
     MHLATHVNPE EVIEQLRNDP EESHRRHVFT LNAVATRTAY STRYASSEEI PKFRIPQLGA
     SAEAVYRLLR DELDLDGIPN LNMASFVGTF MEREAQQLLV ENISKNLADA DEYPALMDLH
     ARCISMIANM WHPRPGEQPI GTATTGSSEA IQLGGLAMKR RWQEKRRAEG KDTSKPNILM
     GANAQVALLK FARYFDVEAR ILDVSENSHY RLDPNDIKKN VDENTIGIFV ILGSTYTGHY
     EPVEELSRIL DQVQEEHGWD IPIHVDAASG GFIAPFVHAG AGGSKWDFEL SRVHSINVSG
     HKFGLVYVGL GWIIWRDRAY LPKDLIFELH YLGGTEESFG LNFSRPGIQV IGQYYNLIRL
     GFDGYREVME NCLQNARLLS KALERTGWYV CVSDIHRKKG DYRFRGVGEI QPHRPGETSA
     DYNEGLPVVA FRFSEQFKKE YPDVKQEAIS LLLRAKQYII PNYPLPPKTD NIEILRVVVR
     ESMSGDLIDK LISDIVEVTE RVMTSEPIDV AVLQSRPTSL ARRHGRLETK LPAKKITKVK
     AGEKACHPMA KGGHRSVC
//