ID   FIXB_ECOUT              Reviewed;         313 AA.
AC   Q1RGF6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Protein FixB {ECO:0000255|HAMAP-Rule:MF_01056};
GN   Name=fixB {ECO:0000255|HAMAP-Rule:MF_01056}; OrderedLocusNames=UTI89_C0048;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Required for anaerobic carnitine reduction. May bring
CC       reductant to CaiA. {ECO:0000255|HAMAP-Rule:MF_01056}.
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_01056}.
CC   -!- SUBUNIT: Heterodimer of FixA and FixB. {ECO:0000255|HAMAP-
CC       Rule:MF_01056}.
CC   -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC       {ECO:0000255|HAMAP-Rule:MF_01056}.
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DR   EMBL; CP000243; ABE05558.1; -; Genomic_DNA.
DR   RefSeq; WP_001091524.1; NC_007946.1.
DR   AlphaFoldDB; Q1RGF6; -.
DR   SMR; Q1RGF6; -.
DR   EnsemblBacteria; ABE05558; ABE05558; UTI89_C0048.
DR   KEGG; eci:UTI89_C0048; -.
DR   HOGENOM; CLU_034178_0_1_6; -.
DR   OMA; RYVFGNK; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000001952; 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_0000300963"
FT   BINDING         255..283
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01056"
SQ   SEQUENCE   313 AA;  33514 MW;  C954EEA35FC30351 CRC64;
     MNTFSQVWVF SDTPSRLPEL MNGAQALANQ INTFVLNDAD GTQAIQLGAN HVWKLSGKPD
     ERMIEDYAGV MADTIRQHGA DGLVLLPNTR RGKLLAAKLG YRLNAAVSND ASAVSVQDGK
     ATVKHMVYGG LAIGEERIAT PYAVLTISSG TFDAAQPDAS RTGETHTVEW QAPAVAITRT
     ATQARQSNSV DLDKARLVVS VGRGIGSKEN IALAEQLCKA IGAELACSRP VAENEKWMEH
     ERYVGISNLM LKPELYLAVG ISGQIQHMVG ANASQTIFAI NKDKNAPIFQ YADYGIVGDA
     VKILPALTVA LAR