ID G2WW33_VERDV Unreviewed; 559 AA.
AC G2WW33;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=VDAG_01819 {ECO:0000313|EMBL:EGY19803.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY19803.1, ECO:0000313|Proteomes:UP000001611};
RN [1] {ECO:0000313|Proteomes:UP000001611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC {ECO:0000313|Proteomes:UP000001611};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
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; DS572697; EGY19803.1; -; Genomic_DNA.
DR RefSeq; XP_009656143.1; XM_009657848.1.
DR AlphaFoldDB; G2WW33; -.
DR STRING; 498257.G2WW33; -.
DR EnsemblFungi; EGY19803; EGY19803; VDAG_01819.
DR GeneID; 20703282; -.
DR KEGG; vda:VDAG_01819; -.
DR eggNOG; KOG1383; Eukaryota.
DR HOGENOM; CLU_019582_2_3_1; -.
DR InParanoid; G2WW33; -.
DR OMA; KNIMQNC; -.
DR OrthoDB; 2783360at2759; -.
DR Proteomes; UP000001611; Chromosome 7.
DR GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR GO; GO:0006538; P:glutamate catabolic process; IEA:EnsemblFungi.
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:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000001611}.
FT REGION 401..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 303
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 559 AA; 62551 MW; EBE086A50EFE2F61 CRC64;
MSLATHVDPD EIIQRLQASH ITAPGHTNLN SQGRAAHIHP FDTQYSSQEN IPKFKIPQDG
APADTVYHMV RNQLDLDGKP NLNLASFVST FLEPNAQQLM EENLTKNLAD SDEYPAMMEI
HQRCISIIAH LWGVQPGERA IGSACTGSSE AIHLGGLAMK RRWQEKRKAE GKDTSKPNII
MGANAQVALE KFARYFEVEA RILPVSAESR FRLDPELVKE NIDENTIGVF VILGSTYTGH
YEPVEEISKI LDDYEAKTGV DIPIHVDAAS GGFIAPFTDA GAGGAKWNFE LPRVKSINTS
GHKFGLVSAG LGWIIWRDEA YLPEFLVFEL HYLGGTEKSY TLNFSRPGAQ VVVQYYNLVH
LGFSGYRGIM ENCLTNARLL ANSLEETGWY TVVSDIHRRV DGGSDRAPKS GTEGAEQEPP
RETSADYVAG LPVVSFRLTD EFQKQYSHIK QETVSLFLRA KGWIIPNYAL PPSEEKTEIL
RVVVRENMTF DLLELLLTDI VTVTETLIED DKVDLSSLKR HHIGHGRRPV TKQDHERHKR
RLEGHGKKRP QDGIHRTVC
//
