(data stored in ACNUC8465 zone)

SWISSPROT: B6HDH9_PENRW

ID   B6HDH9_PENRW            Unreviewed;      1119 AA.
AC   B6HDH9;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 54.
DE   RecName: Full=Bifunctional cytochrome P450/NADPH--P450 reductase {ECO:0000256|PIRNR:PIRNR000209};
DE   Includes:
DE     RecName: Full=Cytochrome P450 {ECO:0000256|PIRNR:PIRNR000209};
DE              EC=1.14.14.1 {ECO:0000256|PIRNR:PIRNR000209};
DE   Includes:
DE     RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000256|PIRNR:PIRNR000209};
DE              EC=1.6.2.4 {ECO:0000256|PIRNR:PIRNR000209};
GN   ORFNames=Pc20g04310 {ECO:0000313|EMBL:CAP85760.1}, PCH_Pc20g04310
GN   {ECO:0000313|EMBL:CAP85760.1};
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:CAP85760.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85760.1, 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   -!- FUNCTION: Functions as a fatty acid monooxygenase.
CC       {ECO:0000256|PIRNR:PIRNR000209}.
CC   -!- CATALYTIC ACTIVITY: NADPH + n oxidized hemoprotein = NADP(+) + n
CC       reduced hemoprotein. {ECO:0000256|PIRNR:PIRNR000209}.
CC   -!- CATALYTIC ACTIVITY: RH + [reduced NADPH--hemoprotein reductase] +
CC       O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.
CC       {ECO:0000256|PIRNR:PIRNR000209}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000209};
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000209};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000209,
CC         ECO:0000256|PIRSR:PIRSR000209-1};
CC   -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome
CC       P450 family. {ECO:0000256|PIRNR:PIRNR000209}.
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DR   EMBL; AM920435; CAP85760.1; -; Genomic_DNA.
DR   RefSeq; XP_002562978.1; XM_002562932.1.
DR   STRING; 500485.XP_002562978.1; -.
DR   EnsemblFungi; CAP85760; CAP85760; PCH_Pc20g04310.
DR   GeneID; 8314528; -.
DR   KEGG; pcs:Pc20g04310; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   eggNOG; KOG1158; Eukaryota.
DR   eggNOG; COG0369; LUCA.
DR   HOGENOM; HOG000093545; -.
DR   KO; K14338; -.
DR   OMA; CEIRFER; -.
DR   OrthoDB; EOG092C08JS; -.
DR   BioCyc; PCHR:PC20G04310-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c20.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR023206; Bifunctional_P450_P450_red.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR003097; FAD-binding_1.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR029039; Flavoprotein-like_dom.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF00067; p450; 1.
DR   PIRSF; PIRSF000209; Bifunctional_P450_P450R; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6HDH9.
DR   SWISS-2DPAGE; B6HDH9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Electron transport {ECO:0000256|PIRNR:PIRNR000209};
KW   FAD {ECO:0000256|PIRNR:PIRNR000209};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR000209};
KW   FMN {ECO:0000256|PIRNR:PIRNR000209};
KW   Heme {ECO:0000256|PIRNR:PIRNR000209, ECO:0000256|PIRSR:PIRSR000209-1};
KW   Iron {ECO:0000256|PIRNR:PIRNR000209, ECO:0000256|PIRSR:PIRSR000209-1};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000209,
KW   ECO:0000256|PIRSR:PIRSR000209-1};
KW   Monooxygenase {ECO:0000256|PIRNR:PIRNR000209};
KW   NADP {ECO:0000256|PIRNR:PIRNR000209};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000209};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Transport {ECO:0000256|PIRNR:PIRNR000209}.
FT   DOMAIN      509    649       Flavodoxin-like. {ECO:0000259|PROSITE:
FT                                PS50902}.
FT   DOMAIN      687    931       FAD-binding FR-type.
FT                                {ECO:0000259|PROSITE:PS51384}.
FT   METAL       414    414       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000209-1}.
SQ   SEQUENCE   1119 AA;  123473 MW;  DF0AFD11C3BB8FAD CRC64;
     MSSTDQVPIP GPKGVPFLGN VYDIEPELPL QSFERMADSY GPIYRLTTFG RARVFVSSHE
     LVDEVCDEER FSKMVSAGLA EIRNGVHDGL FTANYPGEEN WAIAHRILVP AFGPLMIRGM
     FDEMYDIATQ LVMKWARIGP AAPIQVTDDF TRLTLDTIAL CAMGTRFNSF YHDEMHPFVE
     AMVGLLSVSG HRALKPALLN NLPTSENNKY WSDIEYLRNL SKELVDSRKE NPVDKKDLLN
     ALILGRDPQT GRGMTDDSIV DNMITFLIAG HETTSGMLSF LFYHLLKNPS AYRKAQDEVD
     RVIGKRKITV DDMSKLPYIT AVMRETLRLN PTAPMIALHP HPTKNKEDPV TLGGGKYVLN
     GDETIALLLT KMHRDPKVYG PDADEFKPER MLDENFEKLP KNAWKPFGNG MRGCIGRPFA
     WQEALLVVAI LLQNFNFQME NPSYDLRLKQ TLTIKPKDFH MKATLRDGLD PTQLSTTLSG
     SGAGPTETGA ASRDRKPKVA PAGGKLKPMH VFYGSNTGTC EAFARRLADD AAAYGYAAQT
     NSLDSAMQNI PKNDPVVFIS ASYEGQPPDN AAHFFQWLSE LKGSELEGVN YAVFGCGHHD
     WSSTFYRVPK AIDELAKTNG ANKLCDIGLA DAANSDMFTD FDGWGETLFW PGVMAKFGGT
     SPEPAAKPKS SLQVEVSSGM RASTLGLQLE EGFVIENQLL TPPGAPAKRV VKFKLPSDMT
     YQCGDYLAVL PVNPSPVVRR AIRRFDLPWD AVLKVKKPSG STSSPSIPID TPISAFELLS
     TYIELSQPAS KRDLNVLADA AISDAELQAE LRYLASSPSR FTEEIVKKRV SPLDLLIRYP
     SIKLLIGDFL AMLPPMRVRQ YSISSSPLVD PSECSITFTV LSAPALANAT PEGSESIEQY
     LGVASNYLSE LQAGERAHIT VRPSHSGFKP PMDLETPMIM ACAGSGLAPF RGFVMDRAEK
     IRGRRSSPDS DELHESETFK PAKAVLYIGC RTKGQDDIHA AELAEWAALG AVDVRWAYSR
     PADGSKGQHV QDAMLDDREE LVKLFDEGAN IYVCGSTGVG AGIRDACKQM YLERRRAVHA
     ELREKGETPP GADLEEDQAA EQFFDNLRTK ERYATDVFT
//

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