ID A0A383WCI1_TETOB Unreviewed; 1466 AA.
AC A0A383WCI1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=NADPH--hemoprotein reductase {ECO:0000256|ARBA:ARBA00023797};
DE EC=1.6.2.4 {ECO:0000256|ARBA:ARBA00023797};
GN ORFNames=BQ4739_LOCUS15446 {ECO:0000313|EMBL:SZX75141.1};
OS Tetradesmus obliquus (Green alga) (Acutodesmus obliquus).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Scenedesmaceae; Tetradesmus.
OX NCBI_TaxID=3088 {ECO:0000313|EMBL:SZX75141.1, ECO:0000313|Proteomes:UP000256970};
RN [1] {ECO:0000313|EMBL:SZX75141.1, ECO:0000313|Proteomes:UP000256970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Cai Z.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome P450
CC family. {ECO:0000256|ARBA:ARBA00010018}.
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DR EMBL; FNXT01001225; SZX75141.1; -; Genomic_DNA.
DR STRING; 3088.A0A383WCI1; -.
DR Proteomes; UP000256970; Unassembled WGS sequence.
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:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 2.
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; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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:SF17; NADPH--CYTOCHROME 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 PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF48264; Cytochrome P450; 2.
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}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000256970};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 826..994
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 1067..1309
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 779..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1466 AA; 153311 MW; E81C6592C0BB918E CRC64;
MASCTNQHFI YVALAAGLSA AAAYKLLSRS SRHPRIAVFL DGPNGCNKAG FNVQLATGGG
LQQLCSAVCS KAQLHKVTLY GLSSKQQLTE RNLRQLLQAE AAACGGTAVL VAAAGEHQAL
SEATLQQPGL SPVPWGPGWL PLLGHRLALL RGPWGAPFAN LALNLFSGTA GGAAGPTLLL
QVGSPSVGRH LAAAGVVDEA ADGCGVVFTA DPAIAAELLA RQDDFVKMWD RPQQLAVQRI
SDNGLFTSST TSPDWQTARG LLSRGFNTLK LAGYFPLVMD KIRGFLGEWG RYPPGALISG
VNEWLACLTS DAVVVAASGW DMRNLQRKGS GEDVHPFLSA FKFGLRYAFG IISAPEVLGW
RHVLNPLASS AAAMEAQFKH ARKVCEDMVD DMVERTRRGE LGSATSSVLS SLLSEKSPSN
GQYVRQRAVY GHVINLMVAG GGATQHMSAH VCEDMVDDMV ERTRRGELGS ATSSVLSSLL
SEKSPSNGQY VRQRAVYGHV INLMVAGHET TAATLGFLAA YLAAHPAWED AIRTEARAVL
AGRAELSLAD LPRLATAEAC FKEALRLHPP VGMINRDAQA PCMLGSRWLV QRGQRVAVLL
TALHRNEDHW GGKWGSPHQF NPQRFMPGAA ESCGRHACAF MPFGMGVRTC IGQQFALMEA
KAWLASTYDL FTFKLPPGFT FMPSHKEGGA SPNLQGLALQ VFPAPGARTA SAVARVPAFF
GKGAAASSGH HRSDSLSRMH AGAEAACPAV GAGAHVPSPL SQEAAAHFAA AAASAEDTRS
AHSAPAISGR TPTAETASAS QSAAAAAAAA AAAAGGDDEG RHGTPLLVLY GSNAGTCEAF
AELLVEQARL AGFEARTASL DSVITTAAGS SSSSSSSGAA AGGLSARLPR AGALVVVTST
YNGYPPDNAL QFARWLDAAA AAATDGGQGG AAAGLRYAVF GVGSSQWETF HAFPKRVDAR
LAAAGGERLR GLATADVCGC GFADAFEAWQ ADLLAELLAI HNVRVPRKGS AAAAAAAAHG
FASRRRVGLR MLPEASPFPG ASLEAAVATL RGVQGRGMGA DGLPLDFTFS LLRVVRSQEL
QAQGSGRSTK HVELALPQGM AYTAGASHSQ TACCPCCIIS PPXAGALALL GLSGAEAVEW
TPAVTPEAAA RGCVMPPITI SSAQALTWLS DLAAVPTRRQ VLELAELCGC PPEAAALWEL
AAEDNYRQQV SGPRLSVLEL LARHRSLLAA LPLPRLINFL PRIKPRYYSI ASSPRSAPDR
ACVTVARVEL TTPSGRLHRG PGSCTLHDTP VGGFVMGSVS GLVSGFRLPR DPTTPLIMVG
PGTGVAPFMG FMEERQALRQ AGATLGPAVL FFGCRHPAQD YLYQERLEGW RASGVLSGLA
VAFSREGPCK VYVQDLIKQQ GEQLWALLDK QGAAVYVCGD ARRMAPGVAA AFQAVAQEWG
GRSASGAASW LGSLREAKRY LEDVWA
//
