ID Q6BGH8_PARTE Unreviewed; 588 AA.
AC Q6BGH8;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 104.
DE RecName: Full=NADPH--hemoprotein reductase {ECO:0000256|ARBA:ARBA00023797};
DE EC=1.6.2.4 {ECO:0000256|ARBA:ARBA00023797};
GN ORFNames=GSPATT00000510001 {ECO:0000313|EMBL:CAK56074.1}, PTMB.45
GN {ECO:0000313|EMBL:CAH03242.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAH03242.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAH03242.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAH03242.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=15296759; DOI=10.1016/j.cub.2004.07.029;
RA Zagulski M., Nowak J.K., Le Mouel A., Nowacki M., Migdalski A.,
RA Gromadka R., Noel B., Blanc I., Dessen P., Wincker P., Keller A.M.,
RA Cohen J., Meyer E., Sperling L.;
RT "High coding density on the largest Paramecium tetraurelia somatic
RT chromosome.";
RL Curr. Biol. 14:1397-1404(2004).
RN [2] {ECO:0000313|EMBL:CAK56074.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK56074.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
RN [3] {ECO:0000313|EMBL:CAK56074.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK56074.1};
RG Genoscope;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:CAH03242.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAH03242.1};
RA Nowak J.K., Migdalski A., Gromadka R., Zagulski M.;
RT "Paramecium megabase sequencing project.";
RL Submitted (NOV-2006) 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; CR548612; CAH03242.1; -; Genomic_DNA.
DR EMBL; CT867985; CAK56074.1; -; Genomic_DNA.
DR RefSeq; XP_001346869.1; XM_001346833.1.
DR RefSeq; XP_001423472.1; XM_001423435.1.
DR AlphaFoldDB; Q6BGH8; -.
DR STRING; 5888.Q6BGH8; -.
DR EnsemblProtists; CAK56074; CAK56074; GSPATT00000510001.
DR GeneID; 5009256; -.
DR GeneID; 79573983; -.
DR KEGG; ptm:GSPATT00000510001; -.
DR KEGG; ptm:PTMB.45; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_001570_17_3_1; -.
DR InParanoid; Q6BGH8; -.
DR Proteomes; UP000000600; Chromosome.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:GO_Central.
DR CDD; cd06207; CyPoR_like; 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; 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:UP000000600}.
FT DOMAIN 17..160
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 588 AA; 67874 MW; 33109B4D7E34C951 CRC64;
MGCGSSSGSQ LETRGLIYIY YGTTTGNSSR LAFQFASEVR NLKFIPKIIN LSEYNPKEMI
SSKLNVFFVS TYGMGSCTPD TENFDQWLFC EERSKNEFQG MIYLIFALGS TNHEHFCEFG
IRLDKRLEYL GAKRLCNLGK GDAAKDQTEN DYQQWIHTEV QQTLQTQFPL YTCDQGQQDF
STIKIQITKE PEDFQSVNLD FMALKYINSM AFSISEIKEL KALPARGNST LLLDLFNQNI
EYKTAYNIAI YPQNSDSDVD ELCSLLKLDK NVRFKVITNS KQPFPNPISV YTYLKKFCDF
SGLVTKKILI ELSNLVNQKQ LEDELLHLAS FEGRDQYQNR FINQKQNLLN LIKEYQINNL
TLEKIIDICP LIQPRYFTIA SSNKKHPKNI HILASQFVLN QERLGLSSQF FRSLKKGDVV
KGLIQPSKFK YPKNPKAPIL LIGIGAGLAP LRALIQERDY YLEKNQFEKC PFQGGMKLYY
GCRTEAEYLC REELQAYLNS GTLSELKVAF SRKEPKQYVT ELIAIDELYQ HFQMDGLLYI
CGSTELGRDI QVKIADMFEY FENIDPYLTD QKIKELEENS QILTEYWG
//
