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Database: UniProt
Entry: A0A0W7VI40_9HYPO
LinkDB: A0A0W7VI40_9HYPO
Original site: A0A0W7VI40_9HYPO 
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
//
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