ID   B8N3R7_ASPFN            Unreviewed;       608 AA.
AC   B8N3R7;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   SubName: Full=Glutamate decarboxylase, putative {ECO:0000313|EMBL:EED55879.1};
GN   ORFNames=AFLA_031510 {ECO:0000313|EMBL:EED55879.1};
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:EED55879.1, ECO:0000313|Proteomes:UP000001875};
RN   [1] {ECO:0000313|EMBL:EED55879.1, 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   -!- 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; EQ963473; EED55879.1; -; Genomic_DNA.
DR   RefSeq; XP_002374661.1; XM_002374620.1.
DR   AlphaFoldDB; B8N3R7; -.
DR   STRING; 332952.B8N3R7; -.
DR   EnsemblFungi; EED55879; EED55879; AFLA_031510.
DR   VEuPathDB; FungiDB:AFLA_001023; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   HOGENOM; CLU_011856_0_0_1; -.
DR   OMA; RHATYHA; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.170; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES         363
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   608 AA;  65975 MW;  B88326924FFDB4C4 CRC64;
     MTVYRAIIGL WNHDVRLFGS VAIHFSSGSA TVPGTGWVLG SWLFPPRPAA RKKCEVAVED
     LLIPFIRSAD EDPLGQKALE NGVNGANGTH NDLKPSGTSL VDHKKPEELQ SILQLELPEQ
     GTGQDGLVEA LQKVLRYSVN TWHQGFLDKL YASTNAPGVA SELILAALNT NVHVYQVSPA
     LTVIEKFTGK QLASLFGLKG PRAGGISVQG GSASNTTSIV IARNNLFPAT KRDGNGDYRF
     VLFTSAHGHY SIEKAAQMLG LGSSSVWSVP IDKQGRMIPA ELENLVRKAL KENRTPFYVN
     ATAGTTVMGS FDPFDEIAAI CKKYNLWFHV DGSWGGSFVF SKRQRQKLAG AEKADSIAIN
     PHKMLGVPVT CSFLLAADLR RFHRANTLPA GYLFHNEDTE LPEANGCNGA VESELSVDSP
     EVWDLADLTL QCGRRADSLK LFLGWTYYGT AGYEKQIDAA CDIAAHLATL VAENPNFILV
     SENPPPCLQV CFYYAPGGQF LHPRGVVSDE AERGKANSKV TEQVTHAIVS KGFMVDFAPP
     SGDDDVVGNG KFFRCVVNVQ TTKETVEALL QAIEEVGPGI VENMKVQKAQ RKFNRPGERG
     HGPVVHHP
//