ID A0A2H3C6M7_9AGAR Unreviewed; 1058 AA.
AC A0A2H3C6M7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:PBK73968.1};
GN ORFNames=ARMSODRAFT_929424 {ECO:0000313|EMBL:PBK73968.1};
OS Armillaria solidipes.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=1076256 {ECO:0000313|EMBL:PBK73968.1, ECO:0000313|Proteomes:UP000218334};
RN [1] {ECO:0000313|Proteomes:UP000218334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-4 {ECO:0000313|Proteomes:UP000218334};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR000209-1};
CC -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome P450
CC family. {ECO:0000256|ARBA:ARBA00010018}.
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DR EMBL; KZ293419; PBK73968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3C6M7; -.
DR STRING; 1076256.A0A2H3C6M7; -.
DR OrthoDB; 1691317at2759; -.
DR Proteomes; UP000218334; Unassembled WGS sequence.
DR GO; GO:0070330; F:aromatase activity; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:InterPro.
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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Heme {ECO:0000256|PIRSR:PIRSR000209-1};
KW Iron {ECO:0000256|PIRSR:PIRSR000209-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000209-1};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000218334};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 495..635
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 672..901
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 404
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 1058 AA; 117466 MW; 464E353A408E955E CRC64;
MSTAIPQPPT VPFLGNTRDL DRDVPIQSFI LLAKTYGEIY QLDLLGGRKL ICINSHALAN
EISDDKRFKK SFTPALYEVR NLVGDGLFTA FGDESNWGVA HRILMPAFGT MSVRGMLDDM
KDICGQLLLK WERFGPHGVI DPATDFTRVA LDTIAYCTMS YRLNSFYTET QPPFVKSMVD
FLKESFVRSK RPHLVQALMH SATAKYESDQ QTMWELANSI IADRKENPID KKDLLDLMLN
AKDPKTGQGL SEESIGHNLL TFLIAGHETS SGMMTFTIYF LLKNPDKMRK LRAEIDEVLG
GRPLEVGDFD KLPYLIAVMR ESLRLGPTAS SRTAAPIEDT TLGGGKYIVK AGSSLTVQTY
VMHRDPKVWG EDAEEFRPER MMDGKFEALP PNAWQPFGFG LRGCIGRPFA WQEVMLVLTS
VLQKFDLSLA DPSYTLQISQ ALTIKPKDLK IYAKLRTNAP HISSISAVGI KRAYDGPDVT
PHPHITEPTD SKAPLYVLYG SNTGTSEAFA QRIASEAATY SFAAKIGTLD SITGQLPTNG
PIVIVTASFE GEPADNATRF VDWLSNLQGD ELRGVSFTVF GCGNSDWVQT YQKIPKLCDE
LIEKHGGRRL LERGEGDASL GNFFQVFDEY QGKLWKTLSK EYSTTRRAAD VSVIDVKVID
AGDERAESLR QPDTALGRLV ENKILTPTGR PVKRHLEFEL PSRMNYNAGD CLAILPHNPM
RDINRVLSHF GITNEQHVII SSTSPTSLPI GKPVALFEIL SGYVELSQPA TNKDIENIMS
ASSDEATISS LQGLKASYDD EVIAKRFSVL DILDRYPSAS VSLGAFLQMC PPMRVRQYSI
SSSPLWNPQR VTLTVSVIDS PSRSGEERTF LGVASNYLSG LVPGERVRMA VRTCSSLFRL
PADPTVPIVM FCAGSGIAPM RGFMQERAIQ KISGRDVGKA LLFYGCRNPE VDYLYGESDL
KEWEKLGVVE VHLAFSRVAA LSEDSRYVQD RVWHDREVVS DAYHAGAKFF TCGSGQVAKG
IKSKLVEILE TQQGLDHDQA EKRFQQVTQG RYATDIFD
//
