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Database: UniProt
Entry: B6GYA5_PENRW
LinkDB: B6GYA5_PENRW
Original site: B6GYA5_PENRW 
ID   B6GYA5_PENRW            Unreviewed;      1046 AA.
AC   B6GYA5;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   SubName: Full=Pc12g08580 protein {ECO:0000313|EMBL:CAP80485.1};
GN   ORFNames=Pc12g08580 {ECO:0000313|EMBL:CAP80485.1}, PCH_Pc12g08580
GN   {ECO:0000313|EMBL:CAP80485.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   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:CAP80485.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP80485.1, 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., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   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:
CC       Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC         reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC         COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:60344; EC=1.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00036596};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; AM920427; CAP80485.1; -; Genomic_DNA.
DR   RefSeq; XP_002557688.1; XM_002557642.1.
DR   AlphaFoldDB; B6GYA5; -.
DR   STRING; 500485.B6GYA5; -.
DR   GeneID; 8309117; -.
DR   KEGG; pcs:Pc12g08580; -.
DR   VEuPathDB; FungiDB:PCH_Pc12g08580; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   HOGENOM; CLU_003662_1_0_1; -.
DR   OMA; MIVAVNW; -.
DR   OrthoDB; 5488444at2759; -.
DR   BioCyc; PCHR:PC12G08580-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c12.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR   CDD; cd06207; CyPoR_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR19384:SF109; SULFITE REDUCTASE [NADPH] FLAVOPROTEIN COMPONENT; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF01558; POR; 1.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724}.
FT   DOMAIN          659..897
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   1046 AA;  114642 MW;  192C4595A43813C6 CRC64;
     MGSSVPALSA LNGPTYVTAQ TLIQQVAYLL SDKIFSYSPE TFDLDAALKE WTSKGETNSN
     GESPSVKALE TRQGAGNMAL GYLFSQDFDL KKRHIPQGIV ASSATLPYMR AALEQLSLLY
     SVASPVAAHV AAVDYAGEDG LVSDYASTLS LAEDLGLGLV SSGSAHESQH MALFTTLLSS
     VLPSIHIYDG VRVGRDTTRV IDVLDKDGLT RTYETIRKTL DETRNRHLDA QGKVLELLKT
     LNGELGTDYS AFEYHGHSEP TSVLIAFGTV EATLTAQIAR SLAKDGVRVG VVNVRVYRPF
     IEEEFLRVLP QSTKTVAVLG QVASEQAVQE EGVHSALYED VLASLTFATG REHNPACVEI
     KYPRSQRWDL ISAAAAFQRV YDQPILTVNG ETNASLQLLD PASVQEYTFW DVDSSVTEAA
     AQTLSQALGA DSASNVTLSK THDNLVQGGT IRVDIRKSAK IVDAPYAVTG ADVSYVGNIS
     LLNDVDVLAS VKDNAKVIVN APGIKDEDLE KKLPATFKQA VAQRGISVFV VDSSAVEDSS
     LDALVLQASF VRVALPAQEA LAAKKLSSVT GNAEALDNVT KDLEKLLRQI EVPESWKEPE
     GVSEAVQLPK DIIANSFVSF DKNESEPPTL LKDWETAARG LAFKEAYGTR AALRPDLAHK
     TFTVHVKENR RLTPTTYDRN IFHIEFDLGE TGLKYDIGEA LGIHAENDPE DVKNFIAFYG
     LDPDAIVEVP SREDPAVLEN RTVYQALVQN VDIFGRPPKR FYEALAEFAS DEKEKTNLLT
     LGGPDGATEF KRRAEVDTVT FADILLEYPS AHPEFHDIVR IIGPLKRREY SIASCQKVTP
     TSVALMIVAV NWVDPNGRDR FGLATRYLSR LQPGSPITVS VKSSVMKLPP KSTQPLIMAG
     LGTGLAPFRA FVQHRALEKA QGKEIGAVLL YMGSRHQREE YCYGEEWEAY QEAGVITLLG
     AAFSRDQPEK IYIQDRMRQT LPEIIQAYIR EEGAFYLCGP TWPVPDVTAV LEEAIATEAK
     NNGKKVETRK EIEKLKDEER YVLEVY
//
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