ID   Q2TY91_ASPOR            Unreviewed;       514 AA.
AC   Q2TY91;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
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=AO090103000342 {ECO:0000313|EMBL:BAE65782.1};
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE65782.1, ECO:0000313|Proteomes:UP000006564};
RN   [1] {ECO:0000313|EMBL:BAE65782.1, ECO:0000313|Proteomes:UP000006564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007174; BAE65782.1; -; Genomic_DNA.
DR   RefSeq; XP_001826915.1; XM_001826863.2.
DR   AlphaFoldDB; Q2TY91; -.
DR   SMR; Q2TY91; -.
DR   STRING; 510516.Q2TY91; -.
DR   EnsemblFungi; BAE65782; BAE65782; AO090103000342.
DR   GeneID; 5999037; -.
DR   KEGG; aor:AO090103000342; -.
DR   VEuPathDB; FungiDB:AO090103000342; -.
DR   HOGENOM; CLU_019582_2_2_1; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; 2783360at2759; -.
DR   Proteomes; UP000006564; Chromosome 8.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IDA:AspGD.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IMP:AspGD.
DR   GO; GO:0006538; P:glutamate catabolic process; IDA:AspGD.
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:UP000006564}.
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
//