ID A0A0W7VI40_9HYPO Unreviewed; 537 AA.
AC A0A0W7VI40;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=TGAM01_v207317 {ECO:0000313|EMBL:PON23670.1}, TGAMA5MH_08153
GN {ECO:0000313|EMBL:PNP39888.1};
OS Trichoderma gamsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=398673 {ECO:0000313|EMBL:PNP39888.1, ECO:0000313|Proteomes:UP000236546};
RN [1] {ECO:0000313|EMBL:PON23670.1, ECO:0000313|Proteomes:UP000054821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6085 {ECO:0000313|EMBL:PON23670.1,
RC ECO:0000313|Proteomes:UP000054821};
RX PubMed=26893428;
RA Baroncelli R., Zapparata A., Piaggeschi G., Sarrocco S., Vannacci G.;
RT "Draft Whole-Genome Sequence of Trichoderma gamsii T6085, a Promising
RT Biocontrol Agent of Fusarium Head Blight on Wheat.";
RL Genome Announc. 4:e01747-15(2016).
RN [2] {ECO:0000313|EMBL:PNP39888.1, ECO:0000313|Proteomes:UP000236546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A5MH {ECO:0000313|EMBL:PNP39888.1,
RC ECO:0000313|Proteomes:UP000236546};
RA Gardiner D., Kazan K., Vos C., Harvey P.;
RT "Genomes of Trichoderma spp. with biocontrol activity.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:PON23670.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T6085 {ECO:0000313|EMBL:PON23670.1};
RA Baroncelli R.;
RT "Trichoderma gamsii strain T6085, whole genome shotgun sequencing
RT project.";
RL Submitted (AUG-2017) 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:PNP39888.1}.
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DR EMBL; MTYH01000074; PNP39888.1; -; Genomic_DNA.
DR EMBL; JPDN02000027; PON23670.1; -; Genomic_DNA.
DR RefSeq; XP_018659249.1; XM_018807605.1.
DR AlphaFoldDB; A0A0W7VI40; -.
DR STRING; 398673.A0A0W7VI40; -.
DR GeneID; 29987688; -.
DR OrthoDB; 2783360at2759; -.
DR Proteomes; UP000054821; Unassembled WGS sequence.
DR Proteomes; UP000236546; 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:UP000054821}.
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 308
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 537 AA; 59829 MW; BA5D957A8D38E011 CRC64;
MVHLSAVNRS ASVSPGPQMA PAGGSSSLHP DQGLHKSLSQ VKLSSYQDEF TTSVYGSQFA
GQDLPKHSIP GGAMPKDVAY HMIKDHLSLD NNPKLNLASF VTTFMEDEAE KLMTEAFSKN
FIDYEEYPQS ADIQNRCVNM IGELFHAPPG GDSVGTSCIG SSEAIMLGVL AMKRRWKLKR
QAEGKPTDKP NIIMSSAVQV CWEKAARYFE VEEKYVYCTP DRYTIDPQEA VDLVDENTIG
IAVILGTTYT GHYEDVKSIN DLLEEKGLDV SIHVDAASGG FVAPFVLPDL EWDFRLPRVV
SINASGHKYG LVYPGVGWVI WRSHEYLPQD LIFNINYLGA EQSSFTLNFS KGASQVIGQY
YQFIRLGKKG YEAIMSNLTR TADYLTEVLE HDGFVIMSER GGQGLPLVAF RFKNASEGGK
DRHYDEFALA HHLRSRGWVV PAYTMAPHTE GLKMLRVVVR EDFSKSRCDL LIHDIKLCVG
LLDNADEETI KRQEAFIRDH VASHGKSKQN ARHHASKHYK GEDHSLQGKH GKTHAIC
//