ID YDIS_ECOLI Reviewed; 429 AA. AC P77337; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 04-NOV-2026, entry version 156. DE RecName: Full=Probable electron transfer flavoprotein-quinone oxidoreductase YdiS; DE EC=1.5.5.-; GN Name=ydiS; OrderedLocusNames=b1699, JW1689; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9097039; DOI=10.1093/dnares/3.6.363; RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., RA Wada C., Yamamoto Y., Horiuchi T.; RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 28.0-40.1 min region on the linkage map."; RL DNA Res. 3:363-377(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). CC -!- FUNCTION: Probably accepts electrons from YdiQ/YdiR and reduces a CC quinone. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305}; CC -!- SIMILARITY: Belongs to the ETF-QO/FixC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U00096; AAC74769.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15468.1; -; Genomic_DNA. DR PIR; C64928; C64928. DR RefSeq; NP_416214.1; NC_000913.3. DR RefSeq; WP_001278525.1; NZ_CP009789.1. DR AlphaFoldDB; P77337; -. DR SMR; P77337; -. DR BioGRID; 4260294; 238. DR FunCoup; P77337; 763. DR IntAct; P77337; 5. DR STRING; 511145.b1699; -. DR jPOST; P77337; -. DR PaxDb; 511145-b1699; -. DR EnsemblBacteria; AAC74769; AAC74769; b1699. DR GeneID; 946212; -. DR KEGG; ecj:JW1689; -. DR KEGG; eco:b1699; -. DR KEGG; ecoc:C3026_09730; -. DR PATRIC; fig|1411691.4.peg.558; -. DR EchoBASE; EB3735; -. DR eggNOG; COG0644; Bacteria. DR HOGENOM; CLU_050977_0_0_6; -. DR InParanoid; P77337; -. DR OMA; ACIMYGG; -. DR OrthoDB; 103324at2; -. DR PhylomeDB; P77337; -. DR BioCyc; EcoCyc:G6922-MONOMER; -. DR PRO; PR:P77337; -. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0071949; F:FAD binding; IEA:InterPro. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR InterPro; IPR002938; FAD-bd. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR039651; FixC-like. DR InterPro; IPR059103; FixC-like_C. DR NCBIfam; NF007542; fixC; 1. DR NCBIfam; NF007450; PRK10015.1; 1. DR PANTHER; PTHR43624; ELECTRON TRANSFER FLAVOPROTEIN-QUINONE OXIDOREDUCTASE YDIS-RELATED; 1. DR PANTHER; PTHR43624:SF2; ELECTRON TRANSFER FLAVOPROTEIN-QUINONE OXIDOREDUCTASE YDIS-RELATED; 1. DR Pfam; PF26311; ETF-QO_FixC_C; 1. DR Pfam; PF01494; FAD_binding_3; 1. DR PRINTS; PR00420; RNGMNOXGNASE. DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. PE 3: Inferred from homology; KW FAD; Flavoprotein; Oxidoreductase; Reference proteome. FT CHAIN 1..429 FT /note="Probable electron transfer flavoprotein-quinone FT oxidoreductase YdiS" FT /id="PRO_0000200696" FT BINDING 8..22 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255" SQ SEQUENCE 429 AA; 45923 MW; 860789D79EDA6FA2 CRC64; MSDDKFDAIV VGAGVAGSVA ALVMARAGLD VLVIERGDSA GCKNMTGGRL YAHTLEAIIP GFAVSAPVER KVTREKISFL TEESAVTLDF HREQPDVPQH ASYTVLRNRL DPWLMEQAEQ AGAQFIPGVR VDALVREGNK VTGVQAGDDI LEANVVILAD GVNSMLGRSL GMVPASDPHH YAVGVKEVIG LTPEQINDRF NITGEEGAAW LFAGSPSDGL MGGGFLYTNK DSISLGLVCG LGDIAHAQKS VPQMLEDFKQ HPAIRPLISG GKLLEYSAHM VPEGGLAMVP QLVNEGVMIV GDAAGFCLNL GFTVRGMDLA IASAQAAATT VIAAKERADF SASSLAQYKR ELEQSCVMRD MQHFRKIPAL MENPRLFSQY PRMVADIMNE MFTIDGKPNQ PVRKMIMGHA KKIGLINLLK DGIKGATAL //