ID   A0A317W5S4_ASPEC        Unreviewed;       512 AA.
AC   A0A317W5S4;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=BO83DRAFT_305145 {ECO:0000313|EMBL:PWY80981.1};
OS   Aspergillus eucalypticola (strain CBS 122712 / IBT 29274).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448314 {ECO:0000313|EMBL:PWY80981.1, ECO:0000313|Proteomes:UP000246171};
RN   [1] {ECO:0000313|EMBL:PWY80981.1, ECO:0000313|Proteomes:UP000246171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 122712 {ECO:0000313|EMBL:PWY80981.1,
RC   ECO:0000313|Proteomes:UP000246171};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:PWY80981.1}.
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DR   EMBL; MSFU01000004; PWY80981.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317W5S4; -.
DR   VEuPathDB; FungiDB:BO83DRAFT_305145; -.
DR   OrthoDB; 2783360at2759; -.
DR   Proteomes; UP000246171; 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}.
FT   REGION          481..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         291
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   512 AA;  58211 MW;  BD87ABF67CBF775C CRC64;
     MVHLAQVKRD RDVEKTAEGV DSIQLEDDAF YSSVYGTRFA TEQLPSTEMP EREMPREVAY
     RMIKDELSLD GNPMLNLASF VTTYMEEEVE KLMTESFSKN FIDYEEYPQS AEIQNRCVNM
     IARLFNAPTD SDDEHPMGTS TIGSSEAIML GTLAMKRRWQ NKRKAEGKDA SRPNIVMNSA
     VQVCWEKAAR YFDVEERYVY CTEDRYVIDP KQAVDLVDEN TIGICAILGT TYTGEYEDVK
     AINDLLVERG IDCPIHVDAA SGGFVAPFVA PNLEWDFRLS KVVSINVSGH KYGLVYPGVG
     WVVWRSPEYL PKELIFNINY LGAEQASFTL NFSKGASQVI GQYYQMIRLG KRGYRSIMTN
     ITRTADYLAE QLEQLGFVIM SERGGKGLPL VAFRLPADRD SEQFDEFALA HQLRERGWIV
     PAYTMAPNSN SLKLMRVVVR EDFSKNRCDA LLADIKLALK TLSDMDKAML ERYTHHVRVH
     STNSHKSKHV HPHYKNETHS LQGKHGKTHG VC
//