ID   A0A436ZMP0_9PEZI        Unreviewed;       516 AA.
AC   A0A436ZMP0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=DFL_008037 {ECO:0000313|EMBL:RVD80130.1};
OS   Arthrobotrys flagrans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Arthrobotrys.
OX   NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD80130.1, ECO:0000313|Proteomes:UP000283090};
RN   [1] {ECO:0000313|EMBL:RVD80130.1, ECO:0000313|Proteomes:UP000283090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD80130.1,
RC   ECO:0000313|Proteomes:UP000283090};
RA   Youssar L., Wernet V., Hensel N., Hildebrandt H.-G., Fischer R.;
RT   "Intercellular communication is required for trap formation in the
RT   nematode-trapping fungus Duddingtonia flagrans.";
RL   Submitted (JAN-2019) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RVD80130.1}.
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; SAEB01000012; RVD80130.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A436ZMP0; -.
DR   STRING; 97331.A0A436ZMP0; -.
DR   VEuPathDB; FungiDB:DFL_008037; -.
DR   Proteomes; UP000283090; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283090}.
FT   REGION          488..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..505
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         296
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   516 AA;  58305 MW;  48375D238977B16B CRC64;
     MVHLSTIRND AETDTPMAKL MRMSLADDDT PGDTFCSSVY GSRYALEALP TLEMPEEEMP
     KDIAYRLIKD DLSLDGNPML NLASFVTTYM EDEAEKLMHD GLSKNFIDYE EYPQSAEIQN
     RCVNMIGKLF HAPTHEEEEH SIGTSTVGSS EAIMLATLAM KKKWANERKA AGKPFDKPNL
     VMNAAVQVCW EKAARYFDVE ERFVYCTQER YVIDPVQAVD LVDENTIGIC AILGTTYTGE
     YEDVKAINDL LVEKGLNTPI HVDAASGGFV APFVKPDLEW DFRLPRVASI NVSGHKYGLV
     YPGVGWIVWR SPEYLPKELV FNINYLGADQ ASFTLNFSKG ASQIIGQYYQ MIRLGKRGYR
     NIMTNLTRIA DYFSTVLSKR LGFIIMSKGG GDGLPLVAFR LDASKKKHYD EFAIAHHLRE
     RGWIIPAYTM APHSEQLKLM RVVIREDFTK PRCDQLLLDI KHAIDALDSM APKEIEKHAE
     LVNRTVTRTG RRKSHSRHYK GEKHSLAKHG KSQAIC
//