ID A0A1Y2M101_EPING Unreviewed; 522 AA.
AC A0A1Y2M101;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=B5807_07151 {ECO:0000313|EMBL:OSS48908.1};
OS Epicoccum nigrum (Soil fungus) (Epicoccum purpurascens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Epicoccum.
OX NCBI_TaxID=105696 {ECO:0000313|EMBL:OSS48908.1, ECO:0000313|Proteomes:UP000193240};
RN [1] {ECO:0000313|EMBL:OSS48908.1, ECO:0000313|Proteomes:UP000193240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 19927 {ECO:0000313|EMBL:OSS48908.1,
RC ECO:0000313|Proteomes:UP000193240};
RA Fokin M., Fleetwood D., Weir B.S., Villas-Boas S.G.;
RT "Genome sequence of the saprophytic ascomycete Epicoccum nigrum ICMP 19927
RT strain isolated from New Zealand.";
RL Genome Announc. 0:0-0(2017).
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}.
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DR EMBL; KZ107845; OSS48908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2M101; -.
DR STRING; 105696.A0A1Y2M101; -.
DR InParanoid; A0A1Y2M101; -.
DR OMA; RPNLVMG; -.
DR OrthoDB; 2783360at2759; -.
DR Proteomes; UP000193240; 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:UP000193240}.
FT MOD_RES 297
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 522 AA; 59386 MW; EE0C0AA1CD72ED65 CRC64;
MVHVNRVSTD KEIESIKAQY ANIDTIPITE EEEQDDFTAT VYGSKYAGED LPRHEMPERE
MPAAVAHRMI KDDLTLDGTP TLNLASFVTT YMEKEAEDLM VDAFSKNFID YEEYPVSADI
QNRCVSMIAR LFNAPSHDDA NTIGTSTIGS SEAIMLAVLA MKKLWTKKRK AEGKSTENPN
IIMNSAVQVC WEKACRYFDV EEKYVYCTKD RYVIDPKEAV DLVDENTIGI CTILGTTYTG
EYEDTKAIND LLIERNIDVN IHVDAASGGF VAPFVNPELL WDFRLEKVTS INVSGHKYGL
VYPGVGWVVW RDPKYLPKEL IFNINYLGAD QASFTLNFSR GASQIIGQYY QLIRLGKRGY
RRIMLNLTRI ADYLAANLEN LGFIIISQGK GEGLPLVACR LDEDLGKMYD EFAVAHQLRE
RGWVVPAYTM APHSEKMKLM RVVVREDFTK SRCDALISDF RLALETLDKL DAKKIQEHKE
HQFAIRRRTT LHEPVQKKST KEIYGDEDHS LQGKHEKTHA VC
//
