FIXB_ECOLI
ID FIXB_ECOLI Reviewed; 313 AA.
AC P31574; Q2MCG9;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Protein FixB;
GN Name=fixB; Synonyms=yaaR; OrderedLocusNames=b0042, JW0041;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O44:K74;
RX PubMed=7473063; DOI=10.1002/jobm.3620350404;
RA Eichler K., Buchet A., Bourgis F., Kleber H.-P., Mandrand-Berthelot M.-A.;
RT "The fix Escherichia coli region contains four genes related to carnitine
RT metabolism.";
RL J. Basic Microbiol. 35:217-227(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION.
RC STRAIN=K12 / BW25113;
RX PubMed=12081978; DOI=10.1128/jb.184.14.4044-4047.2002;
RA Walt A., Kahn M.L.;
RT "The fixA and fixB genes are necessary for anaerobic carnitine reduction in
RT Escherichia coli.";
RL J. Bacteriol. 184:4044-4047(2002).
CC -!- FUNCTION: Required for anaerobic carnitine reduction. May bring
CC reductant to CaiA. {ECO:0000269|PubMed:12081978}.
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC -!- SUBUNIT: Heterodimer of FixA and FixB. {ECO:0000305}.
CC -!- INTERACTION:
CC P31574; P0AES0: gss; NbExp=2; IntAct=EBI-554030, EBI-557080;
CC P31574; P06993: malT; NbExp=3; IntAct=EBI-554030, EBI-542934;
CC -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC {ECO:0000305}.
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DR EMBL; X71977; CAA50798.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73153.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76037.1; -; Genomic_DNA.
DR PIR; B64725; B64725.
DR RefSeq; NP_414584.1; NC_000913.3.
DR RefSeq; WP_001091499.1; NZ_STEB01000010.1.
DR AlphaFoldDB; P31574; -.
DR SMR; P31574; -.
DR BioGRID; 4262208; 6.
DR BioGRID; 853208; 4.
DR DIP; DIP-9621N; -.
DR IntAct; P31574; 12.
DR STRING; 511145.b0042; -.
DR PaxDb; P31574; -.
DR PRIDE; P31574; -.
DR EnsemblBacteria; AAC73153; AAC73153; b0042.
DR EnsemblBacteria; BAE76037; BAE76037; BAE76037.
DR GeneID; 66671668; -.
DR GeneID; 948939; -.
DR KEGG; ecj:JW0041; -.
DR KEGG; eco:b0042; -.
DR PATRIC; fig|1411691.4.peg.2241; -.
DR EchoBASE; EB1524; -.
DR eggNOG; COG2025; Bacteria.
DR HOGENOM; CLU_034178_0_1_6; -.
DR InParanoid; P31574; -.
DR OMA; RYVFGNK; -.
DR PhylomeDB; P31574; -.
DR BioCyc; EcoCyc:EG11563-MON; -.
DR UniPathway; UPA00117; -.
DR PRO; PR:P31574; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0042413; P:carnitine catabolic process; IMP:EcoCyc.
DR GO; GO:0009437; P:carnitine metabolic process; IMP:EcoliWiki.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
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 1: Evidence at protein level;
KW Electron transport; FAD; Flavoprotein; Reference proteome; Transport.
FT CHAIN 1..313
FT /note="Protein FixB"
FT /id="PRO_0000167861"
FT BINDING 255..283
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 313 AA; 33513 MW; 443DBBD7F97EDE16 CRC64;
MNTFSQVWVF SDTPSRLPEL MNGAQALANQ INTFVLNDAD GAQAIQLGAN 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