ID   A0A319ER02_ASPSB        Unreviewed;       514 AA.
AC   A0A319ER02;
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=BO78DRAFT_403081 {ECO:0000313|EMBL:PYI11681.1};
OS   Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI11681.1, ECO:0000313|Proteomes:UP000248423};
RN   [1] {ECO:0000313|EMBL:PYI11681.1, ECO:0000313|Proteomes:UP000248423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI11681.1,
RC   ECO:0000313|Proteomes:UP000248423};
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 (FEB-2018) 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}.
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DR   EMBL; KZ826317; PYI11681.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319ER02; -.
DR   STRING; 1448318.A0A319ER02; -.
DR   Proteomes; UP000248423; 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:UP000248423}.
FT   REGION          484..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         294
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   514 AA;  58885 MW;  0089D7B024E4FCA1 CRC64;
     MVHLAKVKRD SEIDKTLERV DSIKLESTEE DGFYSSVYGT RFATEQLPST EMPEREMPRE
     VAYRMIKDEL SLDGNPMLNL ASFVTTYMEE EVEKLMTESF SKNFIDYEEY PQSAEIQNRC
     VNMIARLFNA PTDSEEDHPM GTSTIGSSEA IMLGTLAMKR RWQNKRKAEG KDYSRPNIVM
     NSAVQVCWEK AARYFDVEER YVFCTEDRYV IDPQQAVDLV DENTIGICAI LGTTYTGEYE
     DVKAINDLLV ERGIDCPIHV DAASGGFVAP FVNPNLEWDF RLEKVVSINV SGHKYGLVYP
     GVGWVVWRSP EYLPKELIFN INYLGAEQAS FTLNFSKGAS QVIGQYYQMI RLGKRGYRSI
     MVNITRIADY LAEELEKQGF VIMNQRRGKG LPLVAFRLPA ERDTQFDEFA IAHQLRERGW
     IVPAYTMAPN SNQLKLMRVV VREDFTKSRC DALLADIKLA LKTLGDMDKA MLERYTQHVR
     EHSTNSHKAK HTHHHYKNET HSLQGKHGKT HGVC
//