ID A0A024TD11_9STRA Unreviewed; 927 AA.
AC A0A024TD11;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=NADPH--hemoprotein reductase {ECO:0000256|ARBA:ARBA00023797};
DE EC=1.6.2.4 {ECO:0000256|ARBA:ARBA00023797};
GN ORFNames=H310_13706 {ECO:0000313|EMBL:ETV91918.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV91918.1};
RN [1] {ECO:0000313|EMBL:ETV91918.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETV91918.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) 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};
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DR EMBL; KI914006; ETV91918.1; -; Genomic_DNA.
DR RefSeq; XP_008879555.1; XM_008881333.1.
DR AlphaFoldDB; A0A024TD11; -.
DR STRING; 157072.A0A024TD11; -.
DR EnsemblFungi; H310_13706-t26_1; H310_13706-t26_1-p1; H310_13706.
DR EnsemblProtists; ETV91918; ETV91918; H310_13706.
DR GeneID; 20090756; -.
DR VEuPathDB; FungiDB:H310_13706; -.
DR eggNOG; KOG1159; Eukaryota.
DR OrthoDB; 316007at2759; -.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1270.20; -; 2.
DR Gene3D; 3.40.50.2030; -; 1.
DR Gene3D; 3.40.50.360; -; 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; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001226; Flavodoxin_CS.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR004137; HCP/CODH.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR016099; Prismane-like_a/b-sand.
DR InterPro; IPR011254; Prismane-like_sf.
DR InterPro; IPR016100; Prismane_a-bundle.
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; PF03063; Prismane; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF56821; Prismane protein-like; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS00201; FLAVODOXIN; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..143
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 176..416
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 927 AA; 102086 MW; C7FB972553F1F841 CRC64;
MLILYGSQTG TTEAFAKIVH SFATARGLSP RLLVADDFNP TQLVHEGVVI FLTSTFYNGE
FPSNISRTWD YLKATTTSLP STKFAVFGLG NSHNKVNFNV AAKLLDARLE QLGASRLIPL
GLGDEQALCG HETSFRPWIQ HLWMKLLGGH GKMTLPIQFQ ISAPAVDAVS VVRTIPGFNG
FRVVSNALLT PSGYERPTYL LTLELPPDTT YQLGDHIQVS YNNSMELVNR AATRLGLDLN
TTIQLKPFGH SGYLPVDTPI KLVDLLRDYL DLSSPPSRSF LEGLSALCTD PDEALALEQL
AEDMTIGNLY SKYVGGNTVF RTPFTLVDVL ELHPSIQVGL HHILGNISLI RPRYYSVCSS
PLQLPHHVQI VYMVDTWRCS NDPNKVFMGA AAGYMSRLAP GDVVTSLLSR GYFRLPTSLE
TPILGVALGT GISFFRALLQ HRAYHHDHNQ TVSKMRLYFG IRHAAKDFLF QDELTAYVNR
GLLELVPACS HDSKDFVTPV TKIRDFPNEV AQYLDNDGVY FYCGIGGTIP YFHEAAIETA
LQTVHKSTLA AEMETVDEMK LTGRWQVEAF SSCLDHENAL QHQQKVQTKK EDTPISDVVG
DCAMFCFQCG QTNQGIGCTK IGVCGKTPTV AALQDLLVDH LKHLSWYAHH IRAVDPDVAS
LAEIDRFTLV ALFSTLTNVN FDATRFVTFI QQTKGYTDQL TQEYAAVCQA KGVAPSPVPW
KRTEANVVDI EELVASGKKV GVLSRLRAGR NDALVGLQEM LVYGLKGLAA YTDHSLQFGN
EKPEIYHFIH EAFAFLWSPD AGKIDKVVEM LMRCGQVNLT ALALLHESNC TYGAQSPGIA
TSLPRPGKCI LVSGHDLKML HDVLEACAAY KAEHGVHINV YTHGELLPAH GYPALRASPH
LFNLMAIGAD VQQDIANMLD GDKPTAP
//
