ID B7L6H2_ECO55 Unreviewed; 429 AA.
AC B7L6H2;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Protein FixC {ECO:0000256|RuleBase:RU366069};
GN Name=ydiS {ECO:0000313|EMBL:CAU97725.1};
GN OrderedLocusNames=EC55989_1867 {ECO:0000313|EMBL:CAU97725.1};
OS Escherichia coli (strain 55989 / EAEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585055 {ECO:0000313|EMBL:CAU97725.1, ECO:0000313|Proteomes:UP000000746};
RN [1] {ECO:0000313|Proteomes:UP000000746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55989 / EAEC {ECO:0000313|Proteomes:UP000000746};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Part of an electron transfer system.
CC {ECO:0000256|RuleBase:RU366069}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU366069};
CC -!- SIMILARITY: Belongs to the ETF-QO/FixC family.
CC {ECO:0000256|ARBA:ARBA00006796, ECO:0000256|RuleBase:RU366069}.
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DR EMBL; CU928145; CAU97725.1; -; Genomic_DNA.
DR RefSeq; WP_001287813.1; NC_011748.1.
DR AlphaFoldDB; B7L6H2; -.
DR KEGG; eck:EC55989_1867; -.
DR HOGENOM; CLU_050977_0_0_6; -.
DR Proteomes; UP000000746; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR43624; ELECTRON TRANSFER FLAVOPROTEIN-QUINONE OXIDOREDUCTASE YDIS-RELATED; 1.
DR PANTHER; PTHR43624:SF2; ELECTRON TRANSFER FLAVOPROTEIN-QUINONE OXIDOREDUCTASE YDIS-RELATED; 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 {ECO:0000256|RuleBase:RU366069};
KW Flavoprotein {ECO:0000256|RuleBase:RU366069};
KW Oxidoreductase {ECO:0000256|RuleBase:RU366069};
KW Reference proteome {ECO:0000313|Proteomes:UP000000746}.
FT DOMAIN 6..183
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 429 AA; 45981 MW; C045A23100C1758B CRC64;
MSEDKFDAIV 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 QMVNDGVMIV
GDAAGFCLNL GFTVRGMDLA IASAQAAATT VIAAKEREDF SASSLAQYKR ELEQSCVMRD
MQHFRKIPAL IENPRLFSQY PRMVADIMNE MFTIDGKPNQ PVRKMIMGHA KKIGLINLLK
DGIKGATAL
//
