ID   FIXB_ECOL6              Reviewed;         313 AA.
AC   P59674;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-MAY-2003, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Protein FixB;
GN   Name=fixB; OrderedLocusNames=c0051/c0052;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN   [2]
RP   SEQUENCE REVISION.
RA   Plunkett G. III;
RL   Unpublished observations (APR-2003).
CC   -!- FUNCTION: Required for anaerobic carnitine reduction. May bring
CC       reductant to CaiA (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC   -!- SUBUNIT: Heterodimer of FixA and FixB. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC       {ECO:0000305}.
CC   -!- CAUTION: When this sequence was assembled, the third base of codon 137
CC       was missed, generating two ORFs instead of one. {ECO:0000305}.
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DR   EMBL; AE014075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; WP_001091509.1; NZ_CP051263.1.
DR   AlphaFoldDB; P59674; -.
DR   SMR; P59674; -.
DR   OMA; RYVFGNK; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01056; FixB; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR014730; ETF_a/b_N.
DR   InterPro; IPR001308; ETF_a/FixB.
DR   InterPro; IPR014731; ETF_asu_C.
DR   InterPro; IPR018206; ETF_asu_C_CS.
DR   InterPro; IPR023461; FixB.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR43153; PTHR43153; 1.
DR   Pfam; PF01012; ETF; 1.
DR   Pfam; PF00766; ETF_alpha; 1.
DR   PIRSF; PIRSF000089; Electra_flavoP_a; 1.
DR   SMART; SM00893; ETF; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   PROSITE; PS00696; ETF_ALPHA; 1.
PE   3: Inferred from homology;
KW   Electron transport; FAD; Flavoprotein; Transport.
FT   CHAIN           1..313
FT                   /note="Protein FixB"
FT                   /id="PRO_0000167862"
FT   BINDING         255..283
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   313 AA;  33512 MW;  A960554200E4D14D CRC64;
     MNTFSQVWVF SDTPSRLPEL MNGAQALANQ INTFVLNDAD GAQAIQLGAN HVWKLSGKPD
     DRMIEDYADV MADTIRQHGA DGLVLLPNTR RGKLLAAKLG YRLNAAVSND ASAVSVQDGK
     ATVKHMVYGG LAIGEERIAT PYAVLTISSG TFDVAQPDAS RTGETHTVEW QAPAVAITRT
     ATQARQSNSV DLDKARLVVS VGRGIGSKEN IALAEQLCKA IGAELACSRP VAENEKWMEH
     ERYVGISNLM LKPELYLAVG ISGQIQHMVG ANASQTIFAI NKDKNAPIFQ FADYGIVGDA
     VKILPALTAA LAR