CAID_SALTI
ID CAID_SALTI Reviewed; 261 AA.
AC Q8Z9L5;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Carnitinyl-CoA dehydratase {ECO:0000255|HAMAP-Rule:MF_01051};
DE EC=4.2.1.149 {ECO:0000255|HAMAP-Rule:MF_01051};
DE AltName: Full=Crotonobetainyl-CoA hydratase {ECO:0000255|HAMAP-Rule:MF_01051};
GN Name=caiD {ECO:0000255|HAMAP-Rule:MF_01051};
GN OrderedLocusNames=STY0080, t0071;
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 reversible dehydration of L-carnitinyl-CoA to
CC crotonobetainyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01051}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitinyl-CoA = crotonobetainyl-CoA + H2O;
CC Xref=Rhea:RHEA:28338, ChEBI:CHEBI:15377, ChEBI:CHEBI:60932,
CC ChEBI:CHEBI:60933; EC=4.2.1.149; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01051};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_01051}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_01051, ECO:0000305}.
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DR EMBL; AL513382; CAD01224.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO67804.1; -; Genomic_DNA.
DR RefSeq; NP_454680.1; NC_003198.1.
DR RefSeq; WP_000004377.1; NZ_WSUR01000028.1.
DR AlphaFoldDB; Q8Z9L5; -.
DR SMR; Q8Z9L5; -.
DR STRING; 220341.16501353; -.
DR EnsemblBacteria; AAO67804; AAO67804; t0071.
DR KEGG; stt:t0071; -.
DR KEGG; sty:STY0080; -.
DR PATRIC; fig|220341.7.peg.79; -.
DR eggNOG; COG1024; Bacteria.
DR HOGENOM; CLU_009834_7_6_6; -.
DR OMA; AMEMIMT; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.12.10; -; 1.
DR HAMAP; MF_01051; CaiD; 1.
DR InterPro; IPR022852; Carnitinyl_CoA_dehydratase.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Lyase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..261
FT /note="Carnitinyl-CoA dehydratase"
FT /id="PRO_0000109352"
FT ACT_SITE 111
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01051"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01051"
SQ SEQUENCE 261 AA; 28076 MW; EFB0DD88082B5AA5 CRC64;
MSESLHLTRN GPILEITLDR PKANAIDAKT SFAMGEAFLN FRDDPELRVA IITGGGEKFF
SAGWDLKAAA EGEAPDADFG PGGFAGLTEI FDLDKPVIAA VNGYAFGGGF ELALAADFIV
CAENASFALP EAKLGIVPDS GGVLRLPKLL PPAIVNEMVM TGRRMSAEEA LRWGIVNRVV
SQSELMESAR ELAQQLVNSA PLAIAALKEI YRATSEMPVE EGYRYIRSGV LKHYPSVLHS
EDALEGPQAF AEKRAPVWKG R