ID A7AW87_BABBO Unreviewed; 661 AA.
AC A7AW87;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=NADPH--hemoprotein reductase {ECO:0000256|ARBA:ARBA00023797};
DE EC=1.6.2.4 {ECO:0000256|ARBA:ARBA00023797};
GN ORFNames=BBOV_I002330 {ECO:0000313|EMBL:EDO05315.1};
OS Babesia bovis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5865 {ECO:0000313|EMBL:EDO05315.1, ECO:0000313|Proteomes:UP000002173};
RN [1] {ECO:0000313|EMBL:EDO05315.1, ECO:0000313|Proteomes:UP000002173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T2Bo {ECO:0000313|EMBL:EDO05315.1};
RX PubMed=17953480; DOI=10.1371/journal.ppat.0030148;
RA Brayton K.A., Lau A.O.T., Herndon D.R., Hannick L., Kappmeyer L.S.,
RA Berens S.J., Bidwell S.L., Brown W.C., Crabtree J., Fadrosh D.,
RA Feldblum T., Forberger H.A., Haas B.J., Howell J.M., Khouri H., Koo H.,
RA Mann D.J., Norimine J., Paulsen I.T., Radune D., Ren Q., Smith R.K. Jr.,
RA Suarez C.E., White O., Wortman J.R., Knowles D.P. Jr., McElwain T.F.,
RA Nene V.M.;
RT "Genome sequence of Babesia bovis and comparative analysis of apicomplexan
RT hemoprotozoa.";
RL PLoS Pathog. 3:1401-1413(2007).
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 -!- 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:EDO05315.1}.
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DR EMBL; AAXT01000005; EDO05315.1; -; Genomic_DNA.
DR RefSeq; XP_001608883.1; XM_001608833.1.
DR AlphaFoldDB; A7AW87; -.
DR STRING; 5865.A7AW87; -.
DR EnsemblProtists; EDO05315; EDO05315; BBOV_I002330.
DR GeneID; 5477099; -.
DR KEGG; bbo:BBOV_I002330; -.
DR VEuPathDB; PiroplasmaDB:BBOV_I002330; -.
DR eggNOG; KOG1158; Eukaryota.
DR InParanoid; A7AW87; -.
DR Proteomes; UP000002173; Chromosome 1.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 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 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; SSF63380; Riboflavin synthase domain-like; 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}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002173};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..661
FT /note="NADPH--hemoprotein reductase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002707004"
FT DOMAIN 59..204
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT REGION 21..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 661 AA; 76064 MW; FD30DEAA3A707C1F CRC64;
MIITSTVLFY VAYYVWNSNS ESTDDANKKE NDNETNNNTT EKASNTNIEA DNADVSKKIV
VYYGSQTGTA ERFAKTLAHR LADWNSIFQR SSVNLEEFDE HDLLRPNTIA IFLIATHDDG
HFPDNAERFV RWLRLMEDES KRLECLEYCI FGLGSTEYPQ FNNASKNLNN ILINLGAKAL
LPIKLGDDAT DLKSDFEEWS RDVCNALAKR LVIEPVSETF YEKPLLVSLK ETWRDCVPLE
LRYLSKDQIK SDCTPISATV VCKQQWQCVD HVVIDNINMT PESEETTNML TIESYGEFNA
AETINVLYAN PPKVVSYFMD KLNIKEQDME KLITFVPRYA TVDTQMNFEA PFPIPCTIGD
ALRYYLDLTG LPDEETLRNL GTFLQSNHSC QYLNKLFKRK ALMKIMKEEL HLTLQEFIEI
FMHDAIFNIG GFLQIIPKKV TKAYTVSSHP KTNKIDLTIK LVKKRNFTFK TFKSRIQKEI
GYEVRPGTEK MFALHRMYKG ACTHYLCSLQ KGDVVKLYKR PSAFSLISDI FDKPLVMIAN
GSGIAPFRAL WQQGNTTHRR IIFFGFRDEQ HILYKEEIEG LKNMPNYSVN IALSRTGKHE
YVQHILRNHI IQVQDILNSS GLIYVCGSKA MGAQVKAMLQ HFLKIDIAVL KTQQKYVEEL
W
//
