ID FIXB_ECO24 Reviewed; 313 AA.
AC A7ZHD5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Protein FixB {ECO:0000255|HAMAP-Rule:MF_01056};
GN Name=fixB {ECO:0000255|HAMAP-Rule:MF_01056};
GN OrderedLocusNames=EcE24377A_0046;
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000800; ABV16982.1; -; Genomic_DNA.
DR RefSeq; WP_001091505.1; NC_009801.1.
DR AlphaFoldDB; A7ZHD5; -.
DR SMR; A7ZHD5; -.
DR KEGG; ecw:EcE24377A_0046; -.
DR HOGENOM; CLU_034178_0_1_6; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000001122; 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; HUPs; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 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; ELECTRON TRANSFER FLAVOPROTEIN ALPHA; 1.
DR PANTHER; PTHR43153:SF5; PROTEIN FIXB-RELATED; 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; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR PROSITE; PS00696; ETF_ALPHA; 1.
PE 3: Inferred from homology;
KW Electron transport; FAD; Flavoprotein; Reference proteome; Transport.
FT CHAIN 1..313
FT /note="Protein FixB"
FT /id="PRO_1000064382"
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; 33553 MW; BB843557B1D6AE5E CRC64;
MNTFSQVWVF SDTPSRLPEL MNGAQALANQ INTFVLNDAD GAQAIQLGAN HVWKLNGKPD
DRMIEDYAGV MADTIRQHGA DGLVLLPNTR RGKLLAAKLG YRLKVAVSND ASTVSVQDGK
ATVKHMVYGG LAIGEERIAT PYAVLTISSG TFDAAQPDAS RTGETHTVEW QAPAVAITRT
ATQARQSNSV DLDKARLVVS VGRGIGSKEN IALAEQLCKA IGAELACSRP VAENEKWMEH
ERYVGISNLM LKPELYLAVG ISGQIQHMVG ANASQTIFAI NKDKNAPIFQ YADYGIVGDA
VKILPALIAA LAR
//
