ID A0A1J4L2A1_9EUKA Unreviewed; 1103 AA.
AC A0A1J4L2A1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=NADPH--hemoprotein reductase {ECO:0000256|ARBA:ARBA00023797};
DE EC=1.6.2.4 {ECO:0000256|ARBA:ARBA00023797};
GN ORFNames=TRFO_13505 {ECO:0000313|EMBL:OHT16021.1};
OS Tritrichomonas foetus.
OC Eukaryota; Metamonada; Parabasalia; Tritrichomonadida; Tritrichomonadidae;
OC Tritrichomonas.
OX NCBI_TaxID=1144522 {ECO:0000313|EMBL:OHT16021.1, ECO:0000313|Proteomes:UP000179807};
RN [1] {ECO:0000313|Proteomes:UP000179807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K {ECO:0000313|Proteomes:UP000179807};
RA Benchimol M., Almeida L.G., Vasconcelos A.T., Perreira-Neves A., Rosa I.A.,
RA Tasca T., Bogo M.R., de Souza W.;
RL Submitted (OCT-2016) 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 -!- SIMILARITY: Belongs to the NARF family.
CC {ECO:0000256|ARBA:ARBA00006596}.
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:OHT16021.1}.
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DR EMBL; MLAK01000156; OHT16021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4L2A1; -.
DR VEuPathDB; TrichDB:TRFO_13505; -.
DR OrthoDB; 276396at2759; -.
DR Proteomes; UP000179807; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.1780; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 4.10.260.20; Iron hydrogenase, small subunit; 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; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR009016; Fe_hydrogenase.
DR InterPro; IPR004108; Fe_hydrogenase_lsu_C.
DR InterPro; IPR003149; Fe_hydrogenase_ssu.
DR InterPro; IPR036991; Fe_hydrogenase_ssu_sf.
DR InterPro; IPR013352; Fe_hydrogenase_subset.
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 NCBIfam; TIGR02512; FeFe_hydrog_A; 1.
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; PF02906; Fe_hyd_lg_C; 1.
DR Pfam; PF02256; Fe_hyd_SSU; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF13237; Fer4_10; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SMART; SM00902; Fe_hyd_SSU; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53920; Fe-only hydrogenase; 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; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; Iron {ECO:0000256|ARBA:ARBA00022714};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000179807}.
FT DOMAIN 1..78
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 124..152
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 155..184
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 557..693
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 727..992
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1103 AA; 123101 MW; 70B1284DCC1120A7 CRC64;
MSIHVTINGQ SYKAEQGQTI LQVFQSHGIF IPTLCHHPDL PPCGKCGLCV VRIDGGTFVY
ACMQPARNKM IIDTKSADVI EKAKKSLESF FNVSQPPPSP EIEEIVKYLN PKNPVRPREH
DRTNAITFDP TECINCGRCI RICSDILNIG ALNEPNPRMR INECISCGMC ISICPTNSLQ
ETPSIAPILR ALVQNKIIVL QLAPSVRVSV GELFGEPIGT LCTEKIIAAA RQMGISYVLD
TQYGADVTIV EEATELVERL KNKKGLPMFT SCCPSWVNFV ERSHPELTGN LSTTKSPHMI
VGKLIKTYFA DRLRLKETDI FTVSLMPCVS KKDEVKRMQL IGDFDAVITA REFGKMVKDF
GIEWTSLKGG EFDHILGNSS GAGAIFGVSG GVTEATVRYA HEILTGKKIG EIEYHQFRGN
LGSVVKTADI SFGDTVIKMA VCSGISAARD LIESENYKKY HFIEVMSCPG GCIAGGGQPK
LPSRELAINR AKTLYDIDKN QIQNKLKTAA DNTEVTALYK LFLEKPGSHK AHNLLHTHYE
PQETAMLANI KRLQTQPIVG FGSSTGTATR LARIVGGFIK TVSGAMNSLT LTSLIKRKTA
IFIVSTTGDG EFPTNCKKFI ENLRESNIDL SEVRYAVCGL GSRAYNQFCL AGKQLDLIME
EHHAKQIIPF IPIDTSTEDR GETLFERWCL DLCTALGLPP PRIGVNLMYR LTPDNDDSVI
NNPLRPLKFE KMTIKNRSLL TAKNYMKEIF KLDIKMPAGM SYKPGGIFLI FPQNPPEMAK
EVIQVLGYDP NQVFQIHVDA ASVVNFIPER VSIEQLFTMY LDLKGPPNRS LLRAFMRVAN
NEGIEKIQNL LDINNENGFN EYLKDIDIAT CIKQFAQYGV PQIDSLVSSC PHIIPRKYSI
ASAPIKNRGF ISLVVSTLQF GNNRVGLCSD YLRNEKTSKI YMRIMEDEDE DFSELKENPM
ILVATGRGIG SIISILELRQ YDDGPFGKCI LFYGCQSGEG YKPLIDELQE FKKNGAVDEV
YVACSRDTEK KQYVQDAMRE QQDKLWELWQ DPQCSLIYSG FPGTICDDII SIMIEIAETF
GDAAVDEARE FYDNHNVIWR RFD
//
