FIXA_SALPA
ID FIXA_SALPA Reviewed; 256 AA.
AC Q5PIN4;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Protein FixA {ECO:0000255|HAMAP-Rule:MF_01055};
GN Name=fixA {ECO:0000255|HAMAP-Rule:MF_01055}; OrderedLocusNames=SPA0076;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
CC -!- FUNCTION: Required for anaerobic carnitine reduction. May bring
CC reductant to CaiA. {ECO:0000255|HAMAP-Rule:MF_01055}.
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_01055}.
CC -!- SUBUNIT: Heterodimer of FixA and FixB. {ECO:0000255|HAMAP-
CC Rule:MF_01055}.
CC -!- SIMILARITY: Belongs to the ETF beta-subunit/FixA family.
CC {ECO:0000255|HAMAP-Rule:MF_01055}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000026; AAV76110.1; -; Genomic_DNA.
DR RefSeq; WP_000692187.1; NC_006511.1.
DR AlphaFoldDB; Q5PIN4; -.
DR SMR; Q5PIN4; -.
DR EnsemblBacteria; AAV76110; AAV76110; SPA0076.
DR KEGG; spt:SPA0076; -.
DR HOGENOM; CLU_060196_2_2_6; -.
DR OMA; ADLNEWD; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000008185; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01714; ETF_beta; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_01055; FixA; 1.
DR InterPro; IPR000049; ET-Flavoprotein_bsu_CS.
DR InterPro; IPR014730; ETF_a/b_N.
DR InterPro; IPR012255; ETF_b.
DR InterPro; IPR033948; ETF_beta_N.
DR InterPro; IPR023463; FixA.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR21294; PTHR21294; 1.
DR Pfam; PF01012; ETF; 1.
DR PIRSF; PIRSF000090; Beta-ETF; 1.
DR SMART; SM00893; ETF; 1.
DR PROSITE; PS01065; ETF_BETA; 1.
PE 3: Inferred from homology;
KW Electron transport; Transport.
FT CHAIN 1..256
FT /note="Protein FixA"
FT /id="PRO_0000167895"
SQ SEQUENCE 256 AA; 27252 MW; D284763B42D24B17 CRC64;
MKIITCYKCV PDEQDIAINN ADGTLDFSKA DSKISQYDLN AIEAACQLKQ QLGDAQVVAM
SVGGKALTNA KGRKDVLSRG PDELIVVIDD QFEQALPQHT ATALAAAAQK SGFDLLICGD
GSSDLYAQQV GLLVGEALNI PAINGVSKIL SLTDSTLTVE RELEDEVETL SIPLPAVIAV
STDINTPQIP SMKAILGAAK KPVQVWSPAD IGLNSVPAYS TQQVAAPKQR ERQRVVIEGD
GEEQIAAFVE NLRKII