ID   FIXB_ECO8A              Reviewed;         313 AA.
AC   B7M0D9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Protein FixB {ECO:0000255|HAMAP-Rule:MF_01056};
GN   Name=fixB {ECO:0000255|HAMAP-Rule:MF_01056}; OrderedLocusNames=ECIAI1_0044;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
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: 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; CU928160; CAQ96934.1; -; Genomic_DNA.
DR   RefSeq; WP_001091528.1; NC_011741.1.
DR   AlphaFoldDB; B7M0D9; -.
DR   SMR; B7M0D9; -.
DR   KEGG; ecr:ECIAI1_0044; -.
DR   HOGENOM; CLU_034178_0_1_6; -.
DR   OMA; RYVFGNK; -.
DR   UniPathway; UPA00117; -.
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_1000136330"
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;  33541 MW;  D383ABD93F49DE12 CRC64;
     MNTFSQVWVF SDTPSRLPEL MNGAQALANQ INTFVLNDAD GVQAIQLGAN HVWKLNGKPD
     DRMIEDYAGV MADTIRQHGA DGLVLLPNTR RGKLLAAKLG YRLKAAVSND ASTVSVQDGK
     ATVKHMVYGG LAIGEERIAT PYAVLTISSG TFDAAQPDAS RTGETHTVEW QAPAVAITRT
     ATQARQSNSV DLDKARLVVS VGRGIGSKEN IALAEQLCKA IGAELACSRP VAENEKWMEH
     ERYVGISNLM LKPELYLAVG ISGQIQHMVG ANASQTIFAI NKDKNAPIFQ YADYGIVGDA
     VKILPALTAA LAR