ID   A0A1B7NKK0_9EURO        Unreviewed;       466 AA.
AC   A0A1B7NKK0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=ACJ72_08370 {ECO:0000313|EMBL:OAX77334.1};
OS   Emergomyces africanus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX   NCBI_TaxID=1955775 {ECO:0000313|EMBL:OAX77334.1, ECO:0000313|Proteomes:UP000091918};
RN   [1] {ECO:0000313|EMBL:OAX77334.1, ECO:0000313|Proteomes:UP000091918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 136260 {ECO:0000313|EMBL:OAX77334.1,
RC   ECO:0000313|Proteomes:UP000091918};
RA   Cuomo C.A., Schwartz I.S., Kenyon C., de Hoog G.S., Govender N.P.,
RA   Botha A., Moreno L., de Vries M., Munoz J.F., Stielow J.B.;
RT   "Emmonsia species relationships and genome sequence.";
RL   Submitted (JUL-2015) 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:OAX77334.1}.
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DR   EMBL; LGUA01002793; OAX77334.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B7NKK0; -.
DR   STRING; 1658172.A0A1B7NKK0; -.
DR   OrthoDB; 2783360at2759; -.
DR   Proteomes; UP000091918; 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; 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:SF3; 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:UP000091918}.
FT   REGION          426..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..466
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         212
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   466 AA;  52317 MW;  6FC17DF7DD2D8AFE CRC64;
     MEREADELLS ENINKNLADA DEYPALMEMH AHCVSMIANM WHAQPGENAT GSATTGSSEA
     IHLGGLAMKK RWQQRRKAEG KDTSKPNIIM GANAQVALLK FARYFDVEAR LLDVSEESRF
     RLDPELVRKN LDENTIGVFV ILGSTYTGHY EPVEEISDIL DKFEAKTGID VPIHVDAASG
     GFIAPFTYGQ AGGPKWDFLL PRVKSINVSG HKFGLVYAGI GWIIWRDRAY LPEDLVFELH
     YLGGTEETFT LNFSRPGMHV VGQYYNLIRL GFNGYREIME NCLANARLLS MALEKTGWFH
     CVSDIHRKKG NFKFEKVKGL LKYEAGETSA DYNPGLPVVA FRFSDEFQKD YPHVKQDSVS
     LLLRAKQYII PNYPLPPAED KTEILRVVVR ESMSADLIDR LIADIVAITE KLMVTEPMDM
     AALQTGPTSV ARRRMMSKRP GNSGKEKGSK RGVQKHHHKG VHRGVC
//