ID B1LFX7_ECOSM Unreviewed; 428 AA.
AC B1LFX7;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Protein FixC {ECO:0000256|ARBA:ARBA00019877, ECO:0000256|RuleBase:RU366069};
GN Name=fixC {ECO:0000313|EMBL:ACB18829.1};
GN OrderedLocusNames=EcSMS35_0045 {ECO:0000313|EMBL:ACB18829.1};
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855 {ECO:0000313|EMBL:ACB18829.1, ECO:0000313|Proteomes:UP000007011};
RN [1] {ECO:0000313|EMBL:ACB18829.1, ECO:0000313|Proteomes:UP000007011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC {ECO:0000313|Proteomes:UP000007011};
RX PubMed=18708504; DOI=10.1128/JB.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia coli
RT SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(2008).
CC -!- FUNCTION: Could be part of an electron transfer system required for
CC anaerobic carnitine reduction. {ECO:0000256|ARBA:ARBA00037588}.
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; CP000970; ACB18829.1; -; Genomic_DNA.
DR RefSeq; WP_001287705.1; NC_010498.1.
DR AlphaFoldDB; B1LFX7; -.
DR KEGG; ecm:EcSMS35_0045; -.
DR HOGENOM; CLU_050977_0_0_6; -.
DR Proteomes; UP000007011; 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:SF1; PROTEIN FIXC; 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}.
FT DOMAIN 7..185
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 428 AA; 45788 MW; 1D094FB498614514 CRC64;
MSEDIFDAII VGAGLAGSVA ALVLAREGAQ VLVIERGNSA GAKNVTGGRL YAHSLEHIIP
GFADSAPVER LITHEKLAFM TEKSAMTMDY CNGDETSPSQ RSYSVLRSKF DAWLMEQAEE
ADAQLITGIR VDNLVQRDGK VVGVEADGDV IEAKTVILAD GVNSILAEKL GMAKRVKPTD
VAVGVKELIE LPKSVIEDRF QLQGNQGAAC LFAGSPTDGL MGGGFLYTNE NTLSLGLVCG
LHHLHDAKKS VPQMLEDFKQ HPAVAPLIAG GKLVEYSAHV VPEAGINMLP ELVGDGVLIA
GDAAGMCMNL GFTIRGMDLA IAAGEAAAKT VLSAMKSDDF SKQKLAEYRQ HLESGPLRDM
RMYQKLPAFL DNPRMFNGYP ELAVGVARDL FTIDGSAPEL MRKKILRHGK KVGFINLIKD
GMKGVTVL
//
