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Database: UniProt
Entry: B8MXK5_ASPFN
LinkDB: B8MXK5_ASPFN
Original site: B8MXK5_ASPFN 
ID   B8MXK5_ASPFN            Unreviewed;       548 AA.
AC   B8MXK5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 84.
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=AFLA_077920 {ECO:0000313|EMBL:EED57097.1};
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952 {ECO:0000313|EMBL:EED57097.1, ECO:0000313|Proteomes:UP000001875};
RN   [1] {ECO:0000313|EMBL:EED57097.1, ECO:0000313|Proteomes:UP000001875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX   PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963472; EED57097.1; -; Genomic_DNA.
DR   RefSeq; XP_002372709.1; XM_002372668.1.
DR   AlphaFoldDB; B8MXK5; -.
DR   STRING; 332952.B8MXK5; -.
DR   EnsemblFungi; EED57097; EED57097; AFLA_077920.
DR   VEuPathDB; FungiDB:AFLA_003348; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_2_1; -.
DR   OMA; VGWVFWR; -.
DR   Proteomes; UP000001875; 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          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         290
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   548 AA;  62622 MW;  8EC8DF3503D9BC57 CRC64;
     MVHLSRVKRG KQAQKPQQEQ DQGESAASPY VYGTHYATEE LPEHVMSEQE MPADVAFRLI
     KDELSLDGNP LLNLASFVTT YMEDEAQNLM TDAMSKNFID FEEYPQTAHI QNRCINMIAH
     LLNAPTTEGD GELDTIGTST IGSSEAIMLA TLAMKKRWQN KRKAEGKDWT RPNIVMNSAV
     QVCWEKAARY FDVEEKYVYC TDTRYVIDPK TAVDMVDENT IGICAIMGTT YTGQYEDVKA
     INDLLKAKNI DCPIHVDAAS GGFVAPFVRP ELEWDFRLEK VVSINVSGHK YGLVYPGVGW
     VFWRSPEYLP EELIFNVNYL GSNQATFTLN FSKGASHVIG QYYQLIRLGK HGYRSIMQNL
     TKTSDYFADE LKKLGFLIMS DGNGRGLPLV AFRMKPDDDR LYDEFALAHV LRQRGWIVPA
     YTMAPHSNQL KLMRVVLRED FTIHRCNILL EDIKAALKSL QEMDAEMIQK YTLYVLDATN
     GVCKLTRTGT LGRTARRNCH SNMHITKMRS TRCRVKLGRR MVYADFTSRR WVHSKNISCQ
     KAFTYRFQ
//
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