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Database: UniProt/TrEMBL
Entry: E3KD60_PUCGT
LinkDB: E3KD60_PUCGT
Original site: E3KD60_PUCGT 
ID   E3KD60_PUCGT            Unreviewed;       535 AA.
AC   E3KD60;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 2.
DT   05-JUL-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=PGTG_07695 {ECO:0000313|EMBL:EFP82298.2};
OS   Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS   (Black stem rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP82298.2, ECO:0000313|Proteomes:UP000008783};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CRL 75-36-700-3;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E.,
RA   Brockman W., Young S., LaButti K., Sykes S., DeCaprio D., Crawford M.,
RA   Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C.,
RA   Larson L., White J., Zeng Q., Kodira C., Yandava C., Alvarado L.,
RA   O'Leary S., Szabo L., Dean R., Schein J.;
RT   "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL
RT   75-36-700-3.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000008783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRL 75-36-700-3 / race SCCL
RC   {ECO:0000313|Proteomes:UP000008783};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J.,
RA   Cantarel B.L., Chiu R., Coutinho P.M., Feau N., Field M., Frey P.,
RA   Gelhaye E., Goldberg J., Grabherr M.G., Kodira C.D., Kohler A.,
RA   Kuees U., Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E.,
RA   Murat C., Pangilinan J.L., Park R., Pearson M., Quesneville H.,
RA   Rouhier N., Sakthikumar S., Salamov A.A., Schmutz J., Selles B.,
RA   Shapiro H., Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y.,
RA   Rouze P., Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(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:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; DS178281; EFP82298.2; -; Genomic_DNA.
DR   RefSeq; XP_003326717.2; XM_003326669.2.
DR   STRING; 5297.EFP82298; -.
DR   EnsemblFungi; EFP82298; EFP82298; PGTG_07695.
DR   GeneID; 10529671; -.
DR   KEGG; pgr:PGTG_07695; -.
DR   EuPathDB; FungiDB:PGTG_07695; -.
DR   InParanoid; E3KD60; -.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000008783; 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:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR   GO; GO:0006538; P:glutamate catabolic process; IEA:EnsemblFungi.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008783};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008783}.
FT   MOD_RES     296    296       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   535 AA;  60423 MW;  AAE534F9341E5EDF CRC64;
     MSLSKHVKPE QLLQSVKEHG HKTVHGDHHE NISTPYSSRY ASREIPKFKL PSKGIEPDTA
     YQLIHDILDL DGRENANLAS FVHTWAPKQA IQLCVENLGK NLIDQDEYPQ TQILHTRCIS
     MLAHLWHAHN SSNAIGTATT GSSEAIQLGG LAMKKIWQAK RKAAGKSIHE PGPNIVMGAN
     AQVALEKFAR YFDVEMRLVP VSEKTNYCLD PIKAMEYVDE NTIGVFVILG STYTGHFEPV
     KPLSDLLDAY EAKTGISVPI HVDGASGAFI APFVYPDLPW DFRLPRVVSI NTSGHKFGLT
     YVGCGWVVWR DQAHLPKELI FELHYLGSVE YSFSLNFSRP AHPIIHQYYN FVQLGFEGYR
     AIGLDDLANA RLLSRALERS RYYKVLSDIH RKKADMQKPR DQVFGESGLK FEEYVMGLPV
     VAFCWTDEFK KKHPHLKQSW VQTLLRAHAW IVPNYELPPD LEDLQILRVV VRESMSPELV
     DRLFCSIIEI TECLIKEGGP GNFLDAVPKG KSHEHAFGNH QREDATKPVG YARPC
//
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