FIXB_ECO81
ID FIXB_ECO81 Reviewed; 313 AA.
AC B7MNP9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Protein FixB {ECO:0000255|HAMAP-Rule:MF_01056};
GN Name=fixB {ECO:0000255|HAMAP-Rule:MF_01056}; OrderedLocusNames=ECED1_0041;
OS Escherichia coli O81 (strain ED1a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585397;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ED1a;
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; CU928162; CAR06264.1; -; Genomic_DNA.
DR RefSeq; WP_001091515.1; NC_011745.1.
DR AlphaFoldDB; B7MNP9; -.
DR SMR; B7MNP9; -.
DR EnsemblBacteria; CAR06264; CAR06264; ECED1_0041.
DR KEGG; ecq:ECED1_0041; -.
DR HOGENOM; CLU_034178_0_1_6; -.
DR OMA; RYVFGNK; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000000748; 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_1000149640"
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; 33484 MW; 674555420038E3B3 CRC64;
MNTFSQVWVF SDTPSRLPEL MNGAQALANQ INTFVLNDAD GAQAIQLGAN HVWKLSGKPD
ERMIEDYAGV MADTIRQHGA DGLVLLPNTR RGKLLAAKLG YRLNAAVSND ASAVSVQDGK
ATVKHMVYGG LAIGEERIAT PYAVLTISSG TFDVAQPDAS RTGETHTVEW QAPAVAITRT
ATQARQSNSV DLDKARLVVS VGRGIGSKEN IALAEQLCKA IGAELACSRP VAENEKWMEH
ERYVGISNLM LKPELYLAVG ISGQIQHMVG ANASQTIFAI NKDKNAPIFQ YADYGIVGDA
VKILPALTAA LAR