(data stored in ACNUC7421 zone)

SWISSPROT: FIXB_ECODH

ID   FIXB_ECODH              Reviewed;         313 AA.
AC   B1XBG7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 59.
DE   RecName: Full=Protein FixB {ECO:0000255|HAMAP-Rule:MF_01056};
GN   Name=fixB {ECO:0000255|HAMAP-Rule:MF_01056};
GN   OrderedLocusNames=ECDH10B_0043;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(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}.
DR   EMBL; CP000948; ACB01247.1; -; Genomic_DNA.
DR   RefSeq; WP_001091499.1; NC_010473.1.
DR   ProteinModelPortal; B1XBG7; -.
DR   SMR; B1XBG7; -.
DR   EnsemblBacteria; ACB01247; ACB01247; ECDH10B_0043.
DR   KEGG; ecd:ECDH10B_0043; -.
DR   eggNOG; ENOG4105C10; Bacteria.
DR   eggNOG; COG2025; LUCA.
DR   HOGENOM; HOG000247866; -.
DR   KO; K03522; -.
DR   OMA; DMKENTD; -.
DR   UniPathway; UPA00117; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1220; -; 1.
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; B1XBG7.
DR   SWISS-2DPAGE; B1XBG7.
KW   Electron transport; FAD; Flavoprotein; Transport.
FT   CHAIN         1    313       Protein FixB.
FT                                /FTId=PRO_1000136331.
FT   NP_BIND     255    283       FAD. {ECO:0000255|HAMAP-Rule:MF_01056}.
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
//

If you have problems or comments...

PBIL Back to PBIL home page