ID   A1C4D7_ASPCL            Unreviewed;       505 AA.
AC   A1C4D7;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 87.
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=ACLA_059420 {ECO:0000313|EMBL:EAW15277.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW15277.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW15277.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS026990; EAW15277.1; -; Genomic_DNA.
DR   RefSeq; XP_001276703.1; XM_001276702.1.
DR   AlphaFoldDB; A1C4D7; -.
DR   STRING; 344612.A1C4D7; -.
DR   EnsemblFungi; EAW15277; EAW15277; ACLA_059420.
DR   GeneID; 4708796; -.
DR   KEGG; act:ACLA_059420; -.
DR   VEuPathDB; FungiDB:ACLA_059420; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_2_1; -.
DR   OMA; VGWVFWR; -.
DR   OrthoDB; 2783360at2759; -.
DR   Proteomes; UP000006701; 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:SF6; 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:UP000006701}.
FT   MOD_RES         286
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   505 AA;  57216 MW;  0E26ED2215D48455 CRC64;
     MVHLSRVQKR TTPRRHANTK DVTDFVYGTR FAVEDLPRHQ MAEKEMPPEV VYRLVKDELS
     LDGNPMLNLA SFVTTYMEDE VQNLMTDALS KNFIDFEEYP QTSEIQNRCV NMIAELLHAP
     TTADGPDAQD AIGTSTIGSS EAIMLATLAM KRRWQNRRKA EGKDASRPNL IMNTAVHVCW
     EKAARYFDVE EKYVYCTETR FVIDPQEAVD MVDENTIGIC TILGTTYTGQ YEDVKAINDL
     LTERNIDCPI HVDAASGGFV APFVNPSLKW DFQLPKVVSI NISGHKYGLV YPGIGWVFWR
     STEYLPQDLV FNVNYLGSEQ ATFTLNFSKG AANIIGQYYQ LLRLGKHGYR AIMNTLSRIA
     DHLAAELTNL GFIIMSDSGG NNLPLVAYRL PPNEDRLYDE YALAHVLRQR GWIVPAYTMA
     PKANNLKMMR VVLRDDFSMN RCEALIADIK MAMKSLDDMD AQMIQKYMER AAHQNKPLVD
     RQAAPVYQNE KHSLQGKTGK THAIC
//