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}. 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; 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 //