(data stored in SCRATCH zone)

SWISSPROT: B6H1R8_PENRW

ID   B6H1R8_PENRW            Unreviewed;       282 AA.
AC   B6H1R8;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 49.
DE   SubName: Full=Pc13g01530 protein {ECO:0000313|EMBL:CAP91222.1};
GN   ORFNames=Pc13g01530 {ECO:0000313|EMBL:CAP91222.1}, PCH_Pc13g01530
GN   {ECO:0000313|EMBL:CAP91222.1};
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:CAP91222.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP91222.1, 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).
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DR   EMBL; AM920428; CAP91222.1; -; Genomic_DNA.
DR   RefSeq; XP_002558598.1; XM_002558552.1.
DR   ProteinModelPortal; B6H1R8; -.
DR   STRING; 500485.XP_002558598.1; -.
DR   EnsemblFungi; CAP91222; CAP91222; PCH_Pc13g01530.
DR   GeneID; 8307761; -.
DR   KEGG; pcs:Pc13g01530; -.
DR   eggNOG; KOG1577; Eukaryota.
DR   eggNOG; COG0656; LUCA.
DR   HOGENOM; HOG000250272; -.
DR   OMA; APVCWDP; -.
DR   OrthoDB; EOG092C324N; -.
DR   BioCyc; PCHR:PC13G01530-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c13.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd06660; Aldo_ket_red; 1.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR020471; Aldo/keto_reductase.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   PANTHER; PTHR11732; PTHR11732; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; SSF51430; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   4: Predicted;
DR   PRODOM; B6H1R8.
DR   SWISS-2DPAGE; B6H1R8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724}.
FT   DOMAIN       30    265       Aldo_ket_red. {ECO:0000259|Pfam:PF00248}.
FT   ACT_SITE     54     54       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000097-1}.
FT   BINDING     112    112       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000097-2}.
FT   SITE         79     79       Lowers pKa of active site Tyr.
FT                                {ECO:0000256|PIRSR:PIRSR000097-3}.
SQ   SEQUENCE   282 AA;  31597 MW;  417722247D236DF6 CRC64;
     MAPISLQSTY KLVSGYEIPV VGFGVYQTPS DVTEKVTRKA IELGYRHVDS AKVYGNEKES
     AAAIRGSGLD RSKIFYTSKV PSKCMGYEKA KKAIEESIAA ANLGYIDLML IHAPYGGKED
     RLGTWRALVE AQKAGHVRSL GVSNFAIQHL EELEEYIKSG AGGQITVGQY EIHPWCPRED
     IAEWLRKREI IVEAYSPLVQ ATRMKEPVLQ NLAKKHGKTE AQILVRWSLQ KGYVPLPKSV
     TESRILENSQ VFDFTLSDED MASLQLNTYE PVCWDPVRDC KI
//

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