FIXB_SALTY
ID FIXB_SALTY Reviewed; 313 AA.
AC P64095; Q8XH05;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Protein FixB {ECO:0000255|HAMAP-Rule:MF_01056};
GN Name=fixB {ECO:0000255|HAMAP-Rule:MF_01056}; OrderedLocusNames=STM0076;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL19040.1; -; Genomic_DNA.
DR RefSeq; NP_459081.1; NC_003197.2.
DR RefSeq; WP_001032189.1; NC_003197.2.
DR AlphaFoldDB; P64095; -.
DR SMR; P64095; -.
DR STRING; 99287.STM0076; -.
DR PaxDb; P64095; -.
DR EnsemblBacteria; AAL19040; AAL19040; STM0076.
DR GeneID; 1251594; -.
DR KEGG; stm:STM0076; -.
DR PATRIC; fig|99287.12.peg.79; -.
DR HOGENOM; CLU_034178_0_1_6; -.
DR OMA; RYVFGNK; -.
DR PhylomeDB; P64095; -.
DR BioCyc; SENT99287:STM0076-MON; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000001014; 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:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Electron transport; FAD; Flavoprotein; Reference proteome; Transport.
FT CHAIN 1..313
FT /note="Protein FixB"
FT /id="PRO_0000167866"
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
