ID A0A066XFJ3_COLSU Unreviewed; 572 AA.
AC A0A066XFJ3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=CSUB01_09390 {ECO:0000313|EMBL:KDN64775.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN64775.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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:KDN64775.1}.
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DR EMBL; JMSE01001096; KDN64775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XFJ3; -.
DR STRING; 1173701.A0A066XFJ3; -.
DR eggNOG; KOG1383; Eukaryota.
DR HOGENOM; CLU_019582_2_3_1; -.
DR OMA; KNIMQNC; -.
DR OrthoDB; 2783360at2759; -.
DR Proteomes; UP000027238; 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:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238}.
FT REGION 535..559
FT /note="Disordered"
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 572 AA; 64013 MW; 2B233DCA220141D8 CRC64;
MPLSSHVNPE DIVQRLQAAH ITPAGHANIL SQATSAHIQP YDSRYTSQTN IPKYKIPEQG
APGDTVFQMI RDELDLDGKP NLNLASFVGT WMEPNATQLM QENLSKNLSD ADEYPAMMDM
HQRCISIISH LWGVQPGEKA IGSATTGSSE AIHLGGLAMK RRWQIKRKEQ GKDTSKPNIL
MGSNAQVALE KFARYFDVEA RILPVSKKSH YRLDPALVRD NVDENTIGVF VILGSTYTGH
YEPVEEISQI LDKYQEETGI DIPIHVDAAS GGFIAPFTHA GVGGSKWNFE LPRVKSINVS
GHKYGLVYAG LGWIIWRDQS FLPEDLIFEL HYLGGTEKSF TLNFSRPGAQ VIVQYYNLIH
LGFEGYRSIM ENCLSNARLL AESLEATGWY TVVSDIHRPA PNKAASNAAK SVVKQAASTI
GGENTGPRET SADYVAGLPV VSFRLTDEFK NKYRHIQQET ISLMLRARGW IIPNYPLPPN
EEKIEILRVV VRETMTFDLL EHLITDIVEV TETLIEHDEI DLQVLKKHHQ RRRVRVKGDE
ENNKKREGAE GAAKEIGKEV RSMEDGIHRA VC
//