CAIA_SALTI
ID CAIA_SALTI Reviewed; 380 AA.
AC Q8Z9L2;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Crotonobetainyl-CoA reductase {ECO:0000255|HAMAP-Rule:MF_01052};
DE EC=1.3.8.13 {ECO:0000255|HAMAP-Rule:MF_01052};
DE AltName: Full=Crotonobetainyl-CoA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01052};
GN Name=caiA {ECO:0000255|HAMAP-Rule:MF_01052};
GN OrderedLocusNames=STY0083, t0074;
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: Catalyzes the reduction of crotonobetainyl-CoA to gamma-
CC butyrobetainyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01052}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=gamma-butyrobetainyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = crotonobetainyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:51584, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:60933, ChEBI:CHEBI:61513; EC=1.3.8.13;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01052};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01052};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_01052}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01052}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01052}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01052}.
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DR EMBL; AL513382; CAD01227.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO67807.1; -; Genomic_DNA.
DR RefSeq; NP_454683.1; NC_003198.1.
DR RefSeq; WP_000347135.1; NZ_WSUR01000028.1.
DR AlphaFoldDB; Q8Z9L2; -.
DR SMR; Q8Z9L2; -.
DR STRING; 220341.16501356; -.
DR EnsemblBacteria; AAO67807; AAO67807; t0074.
DR KEGG; stt:t0074; -.
DR KEGG; sty:STY0083; -.
DR PATRIC; fig|220341.7.peg.82; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_0_2_6; -.
DR OMA; WACESMI; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0052890; F:oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR HAMAP; MF_01052; CaiA; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR InterPro; IPR023450; CaiA.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; Oxidoreductase.
FT CHAIN 1..380
FT /note="Crotonobetainyl-CoA reductase"
FT /id="PRO_0000201197"
SQ SEQUENCE 380 AA; 42511 MW; 4A7A3965FED6B813 CRC64;
MDFNLNDEQE LFVAGIRELM ASENWEAYFA ECDRDSVYPE RFVKALADMG IDSLLIPEEH
GGLEAGFVTV AAVWMELGRL GAPTYVLYQL PGGFNTFLRE GTQEQIDKIM AFRGTGKQMW
NSAITEPGAG SDVGSLKTTY TRKNGKVYLN GSKCFITSSA YTPYIVVMAR DGASPDKPVY
TEWFVDMSKA GIKVNKLEKL GLRMDSCCEI TFDDVELDEK DMFGREGNGF NRVKEEFDHE
RFLVALTNYG TAMCTFEDAA RYANQRVQFG EAIGRFQLIQ EKFAHMAIKL NSMKNMLLEA
AWKADNGTIT SGDAAMCKYF CANAAFEVVD TAMQVLGGVG IAGNHRITRF WRDLRVDRVS
GGSDEMQILT LGRAVLKQYR
