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Database: UniProt
Entry: W1F4C6_ECOLX
LinkDB: W1F4C6_ECOLX
Original site: W1F4C6_ECOLX 
ID   W1F4C6_ECOLX            Unreviewed;       293 AA.
AC   W1F4C6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Protein FixB {ECO:0000256|HAMAP-Rule:MF_01056};
GN   Name=fixB {ECO:0000256|HAMAP-Rule:MF_01056};
OS   Escherichia coli ISC7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=1432555 {ECO:0000313|EMBL:CDL29191.1, ECO:0000313|Proteomes:UP000019199};
RN   [1] {ECO:0000313|EMBL:CDL29191.1, ECO:0000313|Proteomes:UP000019199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISC7 {ECO:0000313|EMBL:CDL29191.1,
RC   ECO:0000313|Proteomes:UP000019199};
RA   Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., Wiesinger-Mayr H.;
RT   "Antibiotic resistance diversity of beta-lactamase producers in the General
RT   Hospital Vienna.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for anaerobic carnitine reduction. May bring
CC       reductant to CaiA. {ECO:0000256|HAMAP-Rule:MF_01056}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000089-1};
CC       Note=Binds 1 FAD per dimer. {ECO:0000256|PIRSR:PIRSR000089-1};
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_01056}.
CC   -!- SUBUNIT: Heterodimer of FixA and FixB. {ECO:0000256|HAMAP-
CC       Rule:MF_01056}.
CC   -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC       {ECO:0000256|ARBA:ARBA00005817, ECO:0000256|HAMAP-Rule:MF_01056}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDL29191.1}.
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DR   EMBL; CBWN010000146; CDL29191.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1F4C6; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000019199; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW   Rule:MF_01056};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_01056};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_01056};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01056}.
FT   DOMAIN          2..160
FT                   /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00893"
FT   BINDING         183
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         208..209
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         235..263
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01056"
FT   BINDING         240..247
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         261
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ   SEQUENCE   293 AA;  31205 MW;  9366ECA02AA2F7ED CRC64;
     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
//
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