ID A0A0G2EJ73_9PEZI Unreviewed; 773 AA.
AC A0A0G2EJ73;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=UCDDS831_g03574 {ECO:0000313|EMBL:KKY22409.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY22409.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY22409.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY22409.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY22409.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY22409.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-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:RU361171};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU361171}.
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:KKY22409.1}.
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DR EMBL; LAQI01000077; KKY22409.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2EJ73; -.
DR Proteomes; UP000034182; 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: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:RU361171};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU361171}.
FT REGION 519..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..578
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 301
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 773 AA; 87208 MW; D0162C4DFFEEE305 CRC64;
MASLASHIDP DELIQKFHDH PAHHRGFHSS TAVNHNTPYS SRYASISQLS KFKMPHDGAP
ADAVHQMLKD ELDLDGRPNL NLASFVGTYM EEQAEKLMIE NLSKNMSDAD EYPAMMQMHS
RCVSILSHLW GVQKGEKAIG SATTGSSEAI HLGGLAMKRR WQEKRRAEGK STEKPNIIMG
ANAQVALEKF ARYFEVEARI LPVSEKSLYR LDPDLVRENI DENTIGVFVI LGSTYTGHYE
PVEEISKILD EYEAKTGVDI PIHVDGASGA FIAPFTHAQA GGPKWNFELP RVKSINVSGH
KFGLVYAGVG WIIWRDESYL PKHLIFELHY LGGTEESYTL NFSRPGAQII AQYYNLIHLG
FTGYRTIMEN ALSNARLLSR ALEATGWYEC VSDIHRKKGD HKFVEGQKPY EDGENSAAYN
AGLPVVAFTL SKKFKEQFPH VKQVSISNLL RAKQYIIPNY PLPPNEEKTE ILRVVVRESM
SLDLLDRLIT DICAVTETVM QSDEIDLAAW QPFANTIEKT HGSRGVSSRD KHKAKRPMHH
DEDDFSEDDE YSQESDYDSY GEDDEDDDDV NDYDEYYDDY GYDYDEGETP DDSDIGMPDI
ESLSIDDPGF DPAAADPRLC NRCQASERPV PIDMVWCMEF IQTELDNDAQ RAEDAMEVTV
RRLPMVWAWR DFMSYCGVEG VLTPAVRQQT GLGDERAAAQ TLALVEREAL PAIEAWMARR
EGRVWEARAL RQAWVAEGAG RLGPEVVECL WLLSGIVLAW RLGREIDMFA ESL
//
