ID B8NXR9_ASPFN Unreviewed; 514 AA. AC B8NXR9; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 85. 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_008890 {ECO:0000313|EMBL:EED45005.1}, G4B84_011380 GN {ECO:0000313|EMBL:QMW35851.1}; 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:EED45005.1, ECO:0000313|Proteomes:UP000001875}; RN [1] {ECO:0000313|EMBL:EED45005.1, 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}, and NRRL3357 RC {ECO:0000313|EMBL:EED45005.1}; 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). RN [2] {ECO:0000313|EMBL:QMW35851.1, ECO:0000313|Proteomes:UP000515286} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW35851.1, RC ECO:0000313|Proteomes:UP000515286}; RA Fountain J.C., Clevenger J.P., Nadon B., Youngblood R.C., Korani W., RA Chang P.-K., Starr D., Wang H., Isett B., Johnston H.R., Wiggins R., RA Chu Y., Agarwal G., Kemerait R.C., Pandey M.K., Bhatnagar D., RA Ozias-Akins P., Varshney R.K., Scheffler B.E., Vaughn J.N., Guo B.; RT "Two New Chromosome-Level Aspergillus flavus Reference Genomes Reveal a RT Large Insertion Potentially Contributing to Isolate Stress Tolerance and RT Aflatoxin Production."; RL Submitted (JUL-2020) 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EQ963486; EED45005.1; -; Genomic_DNA. DR EMBL; CP059873; QMW35851.1; -; Genomic_DNA. DR RefSeq; XP_002385134.1; XM_002385093.1. DR AlphaFoldDB; B8NXR9; -. DR SMR; B8NXR9; -. DR STRING; 332952.B8NXR9; -. DR EnsemblFungi; EED45005; EED45005; AFLA_008890. DR VEuPathDB; FungiDB:AFLA_013185; -. DR eggNOG; KOG1383; Eukaryota. DR HOGENOM; CLU_019582_2_2_1; -. DR OMA; RPNLVMG; -. DR OrthoDB; 2783360at2759; -. DR Proteomes; UP000001875; Unassembled WGS sequence. DR Proteomes; UP000515286; Chromosome 8. 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 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 //