ID A0A3E2H9Z9_SCYLI Unreviewed; 1065 AA.
AC A0A3E2H9Z9;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=NADPH--hemoprotein reductase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=B7463_g6139 {ECO:0000313|EMBL:RFU30218.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU30218.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU30218.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU30218.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RFU30218.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NCSJ02000106; RFU30218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2H9Z9; -.
DR STRING; 5539.A0A3E2H9Z9; -.
DR OMA; LCTMGFR; -.
DR Proteomes; UP000258309; 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 Electron transport {ECO:0000256|ARBA:ARBA00022982};
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:UP000258309};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 501..642
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 673..903
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 407
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"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU30218.1"
FT NON_TER 1065
FT /evidence="ECO:0000313|EMBL:RFU30218.1"
SQ SEQUENCE 1065 AA; 118764 MW; 2642E789C83F21D3 CRC64;
MTEPIPGPPG LPLLGNMADL NPADATNSLI RFAHIYGPIY KLNLGGEDRI FISSRDLLNE
ICDEKRFQKR VGGALEQIRN GVQDGLFTAY PGEHNWEVAH RVLMPAFGLL SIRAMFDEMY
DIATQLVAKW ARFGPEEIIH VTDDFTRLTL DSIALCAMGT RFNSFYHEEM HPFVTAMVGL
LEESGRRAAR PQIATLFMRS AQKKYDEDIA LLKKVASDLL ADRRAHPNDK KDLLNAMIKG
RDPKTGEGLT DATILNNMIT FLIAGHETTS GMLSFLFYNL LKNPSAYQTA QHEVDEVVGR
GPVTLDHMSK LPYIEACLRE TLRLTPTAPA FTVQAKPDIP EDPVIIGGKY EVKKGQAIAA
ILAECHRDPA VYGPDADEFN PERMLDDNFA KLPPNAWKPF GNGMRGCIGR PFAWQESVLA
VAMLLQNFNF RLHDPAYQLE IKQTLTIKPK DFFMHASLRD HIDPINLEKN LYVPTNEEGK
TTTAEKKVGA SGVPVEHKKP MTILYGSNAG TCEALAQTLA RAATGRGYNV TVDPLDSVVD
KVPENQPVIL ISSSYEGQPP DNAAHFVEWL QKLEDDSKLK NVKYAVYGCG NHDWVSTFHR
IPKLIDSEFQ QHGAKRIAEI GLGDVAKVDI FNEFDRWQDE QLWTQLGGSA DSDHESVLEV
EIDTTTRRSH LRQNLREGIV IDNDLLTAPG EPEKRHISLE LPTGMTYNTG DYLAVLPMNN
PRVIRRVLKR FGLPWDAVIT IKEGANTTLP TGRPISVMDI LSSYVELAQP ATVKHLARIA
ASSSDPAVEA EIKALGPDFE KEITAKRRSP LDLLEKYPAA ALTFGEYLAM LPPMRIRQYS
ISSSPLFSET TVTITWSVLD TPSYAEGDKQ RFLGVASNYL STVEKGERIH VTVKPSHGIF
HPPKDIENTA IIMIGAGSGL APFRGFIQER ACQKAAGRKL APAYLFIGCG HPDKDALFKE
ELEAWQKDGV VEVFYAYSRA SELSKGCRHV QERLWEEREE MTKAFTGGAK LFVCGSSKVG
EGVAETTKKM FRQWCKEVGR DVNDEEVEDW FQKIKSDRYA SDVFA
//
