ID A0A1G2JCV1_9BACT Unreviewed; 435 AA.
AC A0A1G2JCV1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=A2401_03805 {ECO:0000313|EMBL:OGZ84773.1};
OS Candidatus Staskawiczbacteria bacterium RIFOXYC1_FULL_38_18.
OC Bacteria; Candidatus Staskawiczbacteria.
OX NCBI_TaxID=1802229 {ECO:0000313|EMBL:OGZ84773.1, ECO:0000313|Proteomes:UP000177751};
RN [1] {ECO:0000313|EMBL:OGZ84773.1, ECO:0000313|Proteomes:UP000177751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OGZ84773.1}.
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DR EMBL; MHPP01000013; OGZ84773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2JCV1; -.
DR STRING; 1802229.A2401_03805; -.
DR Proteomes; UP000177751; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd06198; FNR_like_3; 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; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
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;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 210..308
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 435 AA; 49235 MW; 6145F6D3EB570CA0 CRC64;
MQNKILARSG WYIIIILSLA PSAFWFLELP ISARFSGASE ATQSLGQIAG LTGMAMFSLM
IILSARLKIF EKVFAGINEA YVAHHFFGGL TFCLLLFHPL LLAYQYLQIS SRAAALFLLP
SAYWPQNFGI IALLITTVTL VITFYIKLKY QIWKFTHKFM GLAFIFAFFH VFLIGSNVGS
NQLLRTYLFI LGMVAIAAFL YRAMFGNYFI RRIPYVVEGV DALPDKIFEV KLVPLGQEMK
FVPGQFVFVK FYSNALTREA HPFSMSSANG NQLKFGIKES GDYTSNIGKL KVGDKAEIEG
PFGAFSFRNH SNRKQAWIAG GVGVTPFMSM LRSLNGEDSG FMIDFYYCVK DEAGFAFRAE
IEEIVKKNKN LRVIFWTTDT MGFINSKVIK NKTPDINNRD VLICGSDIMM SELKKQFLKQ
GINKNQIHTE EFKLY
//
