(data stored in SCRATCH zone)

SWISSPROT: B6H6Y0_PENRW

ID   B6H6Y0_PENRW            Unreviewed;       459 AA.
AC   B6H6Y0;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   05-JUL-2017, entry version 55.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=Pc16g00770 {ECO:0000313|EMBL:CAP92747.1}, PCH_Pc16g00770
GN   {ECO:0000313|EMBL:CAP92747.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP92747.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP92747.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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; AM920431; CAP92747.1; -; Genomic_DNA.
DR   RefSeq; XP_002560496.1; XM_002560450.1.
DR   ProteinModelPortal; B6H6Y0; -.
DR   STRING; 500485.XP_002560496.1; -.
DR   EnsemblFungi; CAP92747; CAP92747; PCH_Pc16g00770.
DR   GeneID; 8315344; -.
DR   KEGG; pcs:Pc16g00770; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   OMA; YTGQYED; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   BioCyc; PCHR:PC16G00770-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c16.
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; 3.40.640.10; -; 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   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6H6Y0.
DR   SWISS-2DPAGE; B6H6Y0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
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:UP000000724}.
FT   MOD_RES     276    276       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   459 AA;  50845 MW;  594DEDA48474DC86 CRC64;
     MGSIEELPKL SGQSKCSYVY GSRFAARPLP SHQLPDGGMP KDVAYQLIKD DLTLDGQPIL
     NLASFVTTYM EDEALKLLAE SANKNIIDHE EYPKSVEIEH RCLNILADLF HSPVSDGAPT
     AFGTSCIGSS EAIMIATLAM KKRWEINRKA QGKDASNPNL IMSSGVQVCW EKAARYFDIA
     EKLVPCTETR YVIDPVQAVD MVDENTIGIC AILGTTYTGQ YEDVQAISEL LIKKGLDTPI
     HVDAASGGFV APFVNPDLVW DFKLPNVVSI NVSGHKYGLV YPGIGWALWR SPEYLPEELV
     FNIDYLGAEQ LNFTMNFSKP ASHIIAQYYQ LIRLGRSGYT SIMKNLTRTA DYLTSQLREM
     GFVIMSEGGG RGLPVVAFRL GSTQNAFLDE WALARKLRER GWIVPAYTMA ADCETMGMMR
     VVVRTDFSMG RCMSLVQDVR DSLGALAGLE IQNIQRYQA
//

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