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Database: UniProt/TrEMBL
Entry: D4D2Q2_TRIVH
LinkDB: D4D2Q2_TRIVH
Original site: D4D2Q2_TRIVH 
ID   D4D2Q2_TRIVH            Unreviewed;       791 AA.
AC   D4D2Q2;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   25-OCT-2017, entry version 36.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=TRV_01358 {ECO:0000313|EMBL:EFE43916.1};
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE43916.1, ECO:0000313|Proteomes:UP000008383};
RN   [1] {ECO:0000313|Proteomes:UP000008383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K.,
RA   Feuermann M., Pedruzzi I., Priebe S., Groth M., Winkler R., Li W.,
RA   Kniemeyer O., Schroeckh V., Hertweck C., Hube B., White T.C.,
RA   Platzer M., Guthke R., Heitman J., Woestemeyer J., Zipfel P.F.,
RA   Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         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
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EFE43916.1}.
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DR   EMBL; ACYE01000073; EFE43916.1; -; Genomic_DNA.
DR   RefSeq; XP_003024527.1; XM_003024481.1.
DR   STRING; 663202.XP_003024527.1; -.
DR   EnsemblFungi; EFE43916; EFE43916; TRV_01358.
DR   GeneID; 9579750; -.
DR   KEGG; tve:TRV_01358; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   eggNOG; COG3535; LUCA.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000008383; 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; 2.40.390.10; -; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR010318; DUF917.
DR   InterPro; IPR024071; DUF917_C.
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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR43321; PTHR43321; 2.
DR   Pfam; PF06032; DUF917; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 2.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008383};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171}.
FT   MOD_RES     534    534       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   791 AA;  88356 MW;  5DD974976F2597A6 CRC64;
     MSLAWRIGRC IARANATNTI STVAEQMIDE VGGPESGKIL FRGKIVAVER RLFKGHSYGE
     ITIQQVLKKE VESSVADELS GDARRSLTPV ATGGVLKIPF KNENIYAKHI SDEGVEKYVA
     TVPDLICVLD TQSGKALGVP EFRYGVMVTV LGIACSPRWS DTERALEIGG PGAFGYKDIK
     YVPLGKYVEP KSVVTEYAER LDIYSTEKEE QAKITPRTYV DPDDIIKHFR EDFDKEQERE
     ASAIFTSNAV SSVTPYSTRY SSKEEIPKFK IPKLGARADA VHHMLSNELD LDGIPNLNMA
     RYMRPSATVD SLKKVTANNC LAYSFVGTYM DREANQLVVE NISKNLADAD EYPALMAIHA
     RCISIISNLW NPQPGEEATG SATTGSSEAI MLGGLAMKKK WQQKRKDEGK DISNPNIIMG
     SNAQVALLKF ARYFDVEARV LDVSEKSQFR LNPELVKKNV DENTIGIFVI LGSTYTGHYE
     PVEEISNILD GIQSETGIDV PIHVDAASGG FVAPFTDAGA GGPKWYSINA SGHKYGLVYA
     GLGWIIWRDR SYLPKELIFE LDYLGSREET YTLNFSRPGA QVIGQYYNFI RLGFNGYREI
     MENCLANARL LSKTLERTGW FVCLSDIHRK KGEFYHQHLN KITPYKEDET SADYNAGLPV
     VTFRFSDAFK ENYPHVKQES ISLLLRSKQY IIPNYPLPPK EQDTEILRVV VRESMAADLI
     DKLVADIAAV TERLMKSDPV DLSALQTGPT NLERRRVRNR EQPHKVSKRP SGKKEKTAGH
     PMRSGIHRSV C
//
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