ID A0A101HIR5_9BACT Unreviewed; 232 AA.
AC A0A101HIR5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE SubName: Full=Putative flavodoxin reductase {ECO:0000313|EMBL:KUK77611.1};
GN ORFNames=XD93_0218 {ECO:0000313|EMBL:KUK77611.1};
OS candidate division WS6 bacterium 34_10.
OC Bacteria; Candidatus Dojkabacteria.
OX NCBI_TaxID=1641389 {ECO:0000313|EMBL:KUK77611.1, ECO:0000313|Proteomes:UP000053904};
RN [1] {ECO:0000313|Proteomes:UP000053904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK77611.1}.
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DR EMBL; LGGO01000019; KUK77611.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101HIR5; -.
DR PATRIC; fig|1641389.3.peg.290; -.
DR Proteomes; UP000053904; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR PRINTS; PR00409; PHDIOXRDTASE.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
FT DOMAIN 4..110
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 232 AA; 26788 MW; F6CF333FF1C9009C CRC64;
MKFNDHYTIE ILEFEQITHD VKRFKTTKPK GYRYTPGQAT EVSINKVGWR DKFRPFTFTS
LNGSDTLEFI IKAYPTNKYP KHTGVTEEIH KLEIGDELII KNPVGTIEYK GKGVFIAGGA
GITPFIAIFR YLENKGRLDG NSLVLSNKKK RDVIIGDELQ QKFNNENLLL TFTREKVEGY
KHRRIDKDML NTLVNDFNQY FYVCGPSGFE NNITDALRAL GAYEEKIVVE EW
//
