(data stored in ACNUC7421 zone)

SWISSPROT: FIXB_ECOL5

ID   FIXB_ECOL5              Reviewed;         313 AA.
AC   Q0TLU7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   11-DEC-2019, entry version 87.
DE   RecName: Full=Protein FixB {ECO:0000255|HAMAP-Rule:MF_01056};
GN   Name=fixB {ECO:0000255|HAMAP-Rule:MF_01056}; OrderedLocusNames=ECP_0042;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG68084.1; -; Genomic_DNA.
DR   RefSeq; WP_001091507.1; NC_008253.1.
DR   SMR; Q0TLU7; -.
DR   PRIDE; Q0TLU7; -.
DR   EnsemblBacteria; ABG68084; ABG68084; ECP_0042.
DR   KEGG; ecp:ECP_0042; -.
DR   eggNOG; ENOG4105C10; Bacteria.
DR   eggNOG; COG2025; LUCA.
DR   HOGENOM; HOG000247866; -.
DR   KO; K03522; -.
DR   OMA; DPHAPIM; -.
DR   BioCyc; ECOL362663:G1G5S-45-MONOMER; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000009182; 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; Q0TLU7.
DR   SWISS-2DPAGE; Q0TLU7.
KW   Electron transport; FAD; Flavoprotein; Transport.
FT   CHAIN           1..313
FT                   /note="Protein FixB"
FT                   /id="PRO_0000300965"
FT   NP_BIND         255..283
FT                   /note="FAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01056"
SQ   SEQUENCE   313 AA;  33508 MW;  9D1286B5CB1336CE CRC64;
     MNTFSQVWVF SDTPSRLPEL MNGAQALANQ INTFVLNDAD GAQAIQLGAN HVWKLNGKPN
     DRMIEDYAGV IADTIRQHGA DGLVLLPNTR RGKLLAAKLG YRLNAAVSND ASTVSVQDGK
     ATVKHMVYGG LAIGEERIAT PYAVLTISSG TFDVAQPDAS RTGETHTVEW QAPAVAITRT
     ATQARQSNSV DLDKARLVVS VGRGIGSKEN IALAEQLCKA IGAELACSRP VAENEKWMEH
     ERYVGISNLM LKPELYLAVG ISGQIQHMVG ANASQTIFAI NKDKNAPIFQ YADYGIVGDA
     VKILPALTAA LAR
//

If you have problems or comments...

PBIL Back to PBIL home page