ID   A6R5Y0_AJECN            Unreviewed;       550 AA.
AC   A6R5Y0;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 85.
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=HCAG_05038 {ECO:0000313|EMBL:EDN08539.1};
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN08539.1, ECO:0000313|Proteomes:UP000009297};
RN   [1] {ECO:0000313|Proteomes:UP000009297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
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}.
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DR   EMBL; CH476659; EDN08539.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6R5Y0; -.
DR   STRING; 339724.A6R5Y0; -.
DR   VEuPathDB; FungiDB:HCAG_05038; -.
DR   HOGENOM; CLU_019582_2_3_1; -.
DR   OMA; KNIMQNC; -.
DR   OrthoDB; 2783360at2759; -.
DR   Proteomes; UP000009297; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009297}.
FT   MOD_RES         302
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   550 AA;  61231 MW;  E3EB8D60DCD42B2C CRC64;
     MTLAAHVDVN QLIEDLRNDP KRRKSERLWT ENVSGSMTPY STRYASHEEI PKFKLPEKGA
     PAEAVRRMLR DDLDLDGIPN LNLASFVGTY MEREADELLF ENISKNLADA DEYPALMEMH
     AHCVSMISNL WHAQPGEHAI GSATTGSSEA ILLGGLAMKK RWQETKKAAG KDTSKPNIIM
     GANAQVALLK FARYFDVEAR ILDVSQKSEY RLDPDLVKKN LDENTIGVFV IMGSTYTGHY
     EPVEEISNIL DEFEAKTGID VPIHVDGASG AFVAPFTYAQ AGGPKWDFAL PRVKSINTSG
     HKFGLVYAGL GWIVWRDRTY LPSDLIFELH YLGGTEETFT LNFSRPGMQV VGQYYNFIRL
     GFNGYREIME NCLANARLLS TALENTGWFL CISGIHRKNG SSKVEQTNGL LKYQEGETSA
     DYNAGLPVVS FRFSDEVQQK YPDVKQESVS LLLRAKQYII PNYPLPPAED KTETLRIVVR
     ESMSADLIDR LVADIVAVTE RLMASEPVDV AALQTGPTSI ARRLVSTVLE NKSAISSIGM
     IFAWNRGGCH
//