ID A0A0A2KE76_PENIT Unreviewed; 1103 AA.
AC A0A0A2KE76;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=PITC_072430 {ECO:0000313|EMBL:KGO65248.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO65248.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO65248.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO65248.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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 ECO:0000256|PIRNR:PIRNR000209};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:142491; EC=1.14.14.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001025,
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|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR000209, ECO:0000256|PIRSR:PIRSR000209-1};
CC -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome P450
CC family. {ECO:0000256|ARBA:ARBA00010018, ECO:0000256|PIRNR:PIRNR000209}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGO65248.1}.
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DR EMBL; JQGA01001515; KGO65248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KE76; -.
DR STRING; 40296.A0A0A2KE76; -.
DR HOGENOM; CLU_001570_7_0_1; -.
DR OMA; DIMGPWE; -.
DR OrthoDB; 1691317at2759; -.
DR PhylomeDB; A0A0A2KE76; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
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 GO; GO:0043386; P:mycotoxin biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd06206; bifunctional_CYPOR; 1.
DR CDD; cd11068; CYP120A1; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR023206; Bifunctional_P450_P450_red.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19384:SF127; BIFUNCTIONAL CYTOCHROME P450_NADPH--P450 REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
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; Cytochrome P450; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR000209};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000209};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000209};
KW FMN {ECO:0000256|ARBA:ARBA00022643, 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|ARBA:ARBA00023033,
KW ECO:0000256|PIRNR:PIRNR000209};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000209};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000209};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000209}.
FT DOMAIN 532..674
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 792..947
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 437
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000209-1"
SQ SEQUENCE 1103 AA; 124328 MW; ACA6FDF2A2886BA6 CRC64;
MMTATRECPA HTLRASASKS APTNDGIDTS KLVEIPTPPP QHYFGLLGHI PEVDPSFPLS
SYWKMMDMYG PIFKLNLGTA TPRILVGNHE LLSEMLDDDR FQKSPNRVQQ AMRDFMGDGL
FTARLEEDNW WKAHRILVPA FGPLGLRKMF DDMLEISSQL ILKWDRFGPA HEIDSAEDFT
RLTFDTIGVC GFGYRFNEFY SEQPHPFAQQ LQEALLESGK MGNRPPFLNP FYYRSEQHRQ
DNIAKMRSLS DEVVQERIAN PNPDAKDVLN LMLTGVDPVS GEKLSVENVQ FQMVTFLGAG
HETTSASLGF TYYYLCNHPE KLLKAQQEVD QVVGDQILTP DMLPKLVYLD ACIKESLRVM
SPINLFNRTA KMDTVLAGKY LIKKGQLISG LMRHFHRDPK IWGDDPDDFR PERMLNGGFE
ALPRNSWKAF GDGLRACIGS GFAVQEMLIN MAMVLQRFHI EKANPDYELK LKSTLSIKPL
EFKMKVRRRQ GRNLMTGIPG GGPVQSGEIS RDQPGSKHRP TIFAENGARQ RVSFFFAGNM
GTSESLAYSL VTTAADFGLD LDIQNLDAAT ENLPSDRPSV FITPSYEGRP PDNGKKFVAW
IEQLAAKSQK LPTGIKYAVF GLGNSDWGNT FHRIPRLVDR LLAQLGAERV IEPVFADVKR
DLLGPWEDWS KQLCMALAGI TEVPGQRSIG VDVQLDKNYA LQAAPREDMA VGTVINHNVL
ADDSVGASKH HLEILLPSQY EYTSGDYLVV EGRNSQEIVS RVIARFNIGR NDGMRVHGSK
KDFLPSQPIS VTEFLQSKVE LATPITKGQL STLALWAEQN SEEHEFLVKL QEEERYQELL
DKRYSIIDVL EEVIRLPLPF GVYIDLLLPS APRQYSISSS SLDPANNRYN EGEHSVIASV
TFDLFNSPAM SGHGTFCGMA SSYLASQKQG DRISCSIRSS NVGFRLPAES EKPVIMLAAG
TGIAPMRAFI QERAAIKSAG VRKLGPAVLL FGCRYPDKDY LYKSELEQWE SQGIVDVIPC
FSRIPEREER RHVPDTLWEL RDRIWEMFQN DGRIYVCGSA SKLGRSCAQT WRRIWMEKMS
QGEVEAEEWL EQIKHTRYIS DVY
//
