(data stored in ACNUC7421 zone)

SWISSPROT: FIXB_ECO27

ID   FIXB_ECO27              Reviewed;         313 AA.
AC   B7UI88;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=Protein FixB {ECO:0000255|HAMAP-Rule:MF_01056};
GN   Name=fixB {ECO:0000255|HAMAP-Rule:MF_01056};
GN   OrderedLocusNames=E2348C_0043;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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}.
DR   EMBL; FM180568; CAS07591.1; -; Genomic_DNA.
DR   RefSeq; WP_001091509.1; NC_011601.1.
DR   SMR; B7UI88; -.
DR   PRIDE; B7UI88; -.
DR   EnsemblBacteria; CAS07591; CAS07591; E2348C_0043.
DR   KEGG; ecg:E2348C_0043; -.
DR   KO; K03522; -.
DR   OMA; DPHAPIM; -.
DR   BioCyc; ECOL574521:E2348C_RS00225-MONOMER; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000008205; 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   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;
DR   PRODOM; B7UI88.
DR   SWISS-2DPAGE; B7UI88.
KW   Complete proteome; Electron transport; FAD; Flavoprotein; Transport.
FT   CHAIN         1    313       Protein FixB.
FT                                /FTId=PRO_1000149638.
FT   NP_BIND     255    283       FAD. {ECO:0000255|HAMAP-Rule:MF_01056}.
SQ   SEQUENCE   313 AA;  33512 MW;  A960554200E4D14D CRC64;
     MNTFSQVWVF SDTPSRLPEL MNGAQALANQ INTFVLNDAD GAQAIQLGAN HVWKLSGKPD
     DRMIEDYADV MADTIRQHGA DGLVLLPNTR RGKLLAAKLG YRLNAAVSND ASAVSVQDGK
     ATVKHMVYGG LAIGEERIAT PYAVLTISSG TFDVAQPDAS RTGETHTVEW QAPAVAITRT
     ATQARQSNSV DLDKARLVVS VGRGIGSKEN IALAEQLCKA IGAELACSRP VAENEKWMEH
     ERYVGISNLM LKPELYLAVG ISGQIQHMVG ANASQTIFAI NKDKNAPIFQ FADYGIVGDA
     VKILPALTAA LAR
//

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