ID Q9UVD7_ASPOZ Unreviewed; 514 AA.
AC Q9UVD7;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 128.
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 Name=GAD {ECO:0000313|EMBL:BAA88152.1};
GN ORFNames=OAory_01046690 {ECO:0000313|EMBL:OOO08169.1};
OS Aspergillus oryzae (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5062 {ECO:0000313|EMBL:BAA88152.1};
RN [1] {ECO:0000313|EMBL:BAA88152.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12596854; DOI=10.1271/bbb.66.2600;
RA Kato Y., Kato Y., Furukawa K., Hara S.;
RT "Cloning and nucleotide sequence of the glutamate decarboxylase-encoding
RT gene gadA from Aspergillus oryzae.";
RL Biosci. Biotechnol. Biochem. 66:2600-2605(2002).
RN [2] {ECO:0000313|EMBL:OOO08169.1, ECO:0000313|Proteomes:UP000190312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC7051 {ECO:0000313|EMBL:OOO08169.1,
RC ECO:0000313|Proteomes:UP000190312};
RA Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA Jeennor S., Laoteng K.;
RT "Genome sequencing of Aspergillus oryzae BCC7051.";
RL Submitted (OCT-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}.
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DR EMBL; AB025422; BAA88152.1; -; Genomic_DNA.
DR EMBL; MKZY01000006; OOO08169.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9UVD7; -.
DR SMR; Q9UVD7; -.
DR VEuPathDB; FungiDB:AO090103000342; -.
DR eggNOG; KOG1383; Eukaryota.
DR OMA; RPNLVMG; -.
DR Proteomes; UP000190312; 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:UP000190312}.
FT REGION 483..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; 58660 MW; 1B10E19A93F28AA5 CRC64;
MVHLAQVHRN ADLDSTIKRV DSIQLENTDE DGFYSSVYGT RFATEQLPQT EMPEREMPRE
VAYRMIKDEL SLDGNPMLNL ASFVTTYMED EAEKLMTESF SKNFIDYEEY PQSAEIQNRC
VNMIARLFNA PVHSEDEHPM GTSTIGSSEA IMLGTLAMKR RWQNKRKAEG KDYSRPNIVM
NSAVQVCWEK AARYFDVEER YVYCTEDRYV IDPQQAVDLV DENTIGICAI LGTTYTGEYE
DVKAINDLLI ERNIDVPIHV DAASGGFVAP FINPKLEWDF RLPKVVSINV SGHKYGLVYP
GVGWVVWRSP EYLPKDLIFN INYLGAEQAS FTLNFSKGAS QVIGQYYQMI RLGKRGYRSI
MTNITVTADF LAQELEKMGF IIMSQRRGHG LPLVAFRLPA EREGQFDEFA LAHQLRERGW
IVPAYTMAPN SNNLKLMRVV VREDFTKSRC DALLSDIKLG LKTLGDMDKA MLDKYTQHVR
THATHSHKSK HNHPHYKGET HSLQGKHGKT HGVC
//
