FIXB_SALTI
ID FIXB_SALTI Reviewed; 313 AA.
AC P64096; Q8XH05;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Protein FixB {ECO:0000255|HAMAP-Rule:MF_01056};
GN Name=fixB {ECO:0000255|HAMAP-Rule:MF_01056};
GN OrderedLocusNames=STY0086, t0077;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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}.
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DR EMBL; AL513382; CAD01230.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO67810.1; -; Genomic_DNA.
DR RefSeq; NP_454686.1; NC_003198.1.
DR RefSeq; WP_001032189.1; NZ_WSUR01000028.1.
DR AlphaFoldDB; P64096; -.
DR SMR; P64096; -.
DR STRING; 220341.16501359; -.
DR EnsemblBacteria; AAO67810; AAO67810; t0077.
DR KEGG; stt:t0077; -.
DR KEGG; sty:STY0086; -.
DR PATRIC; fig|220341.7.peg.86; -.
DR eggNOG; COG2025; Bacteria.
DR HOGENOM; CLU_034178_0_1_6; -.
DR OMA; RYVFGNK; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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 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 3: Inferred from homology;
KW Electron transport; FAD; Flavoprotein; Transport.
FT CHAIN 1..313
FT /note="Protein FixB"
FT /id="PRO_0000167865"
FT BINDING 255..283
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01056"
SQ SEQUENCE 313 AA; 33223 MW; 087C803076FD3871 CRC64;
MNKFSSVWVF SDTPSRLPEL MSGAQAVGEK VNAFVLNEAD SATACHLGAD HVWLLSGKPE
DRMIEDYAAA MAETIRQHSE GGAVLLPNTR RGKLLAAKLG YRLSAAVSND ASDVSLQDGK
AAVKHMVYGG LAIGAETIAS PFAVITLSSG TFDAQQPDAS RSGEMHTVQW QAPATAVTRT
ATQARQSNSV DLDKARLVVS VGRGIGSKEN ISLAEALCQT IGAELACSRP VAENEKWMEH
ERYVGISNLM LKPELYLAVG ISGQIQHMVG ANGAQTIFAI NKDKNAPIFQ YADFGIVGDA
LKILPALTAA LAR