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Database: UniProt
Entry: A0A1F6LI40_9BACT
LinkDB: A0A1F6LI40_9BACT
Original site: A0A1F6LI40_9BACT 
ID   A0A1F6LI40_9BACT        Unreviewed;       231 AA.
AC   A0A1F6LI40;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN   ORFNames=A2725_04335 {ECO:0000313|EMBL:OGH58945.1};
OS   Candidatus Magasanikbacteria bacterium RIFCSPHIGHO2_01_FULL_33_34.
OC   Bacteria; Candidatus Magasanikbacteria.
OX   NCBI_TaxID=1798671 {ECO:0000313|EMBL:OGH58945.1, ECO:0000313|Proteomes:UP000177067};
RN   [1] {ECO:0000313|EMBL:OGH58945.1, ECO:0000313|Proteomes:UP000177067}
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|PIRSR:PIRSR006816-1};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR006816-1};
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:OGH58945.1}.
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DR   EMBL; MFPS01000008; OGH58945.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6LI40; -.
DR   Proteomes; UP000177067; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
DR   CDD; cd00322; FNR_like; 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; IPR012165; Cyt_c3_hydrogenase_gsu.
DR   InterPro; IPR017927; FAD-bd_FR_type.
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; PF00175; NAD_binding_1; 1.
DR   PIRSF; PIRSF006816; Cyc3_hyd_g; 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   FAD {ECO:0000256|PIRSR:PIRSR006816-1};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR006816-1}.
FT   DOMAIN          2..104
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         54..57
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-1"
SQ   SEQUENCE   231 AA;  26595 MW;  65196AAC08B9ED82 CRC64;
     MSTQYKVKLL EKRLITDDVI SLVVEKPSNF DYKAGQFSQI MIPNPENSEK FLKRSYSICS
     TPEENNIEFC IKLLPEGVGS NYLRQVKVGD EIDLVGPFGK FVLKEEKPLV LVATGVGMAP
     IFGLIKDSLI NKNYKEKIHL LFGLRHDKDI FFTNELDKLK EKFDNFDYTL TLSQPSEEWS
     GNKGRVTDYI QKHINNTAHY YICGNIKMIT EIKQILSDLS IEKENIHFEA F
//
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