ID   CAID_ECOSM              Reviewed;         261 AA.
AC   B1LFW9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=EcSMS35_0037;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC;
RX   PubMed=18708504; DOI=10.1128/jb.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(2008).
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}.
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DR   EMBL; CP000970; ACB19722.1; -; Genomic_DNA.
DR   RefSeq; WP_001361348.1; NC_010498.1.
DR   AlphaFoldDB; B1LFW9; -.
DR   SMR; B1LFW9; -.
DR   EnsemblBacteria; ACB19722; ACB19722; EcSMS35_0037.
DR   KEGG; ecm:EcSMS35_0037; -.
DR   HOGENOM; CLU_009834_7_6_6; -.
DR   OMA; AMEMIMT; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000007011; 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   CHAIN           1..261
FT                   /note="Carnitinyl-CoA dehydratase"
FT                   /id="PRO_1000136258"
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;  28153 MW;  D2BC39DD3809E5B6 CRC64;
     MSESLHLTRN GSILEITLDR PKANAIDAKT SFEMGEVFLN FRDDPQLRVA IITGAGEKFF
     SAGWDLKAAA EGEAPDADFG PGGFAGLTEI FNLDKPVIAA VNGYAFGGGF ELALAADFIV
     CADNASFALP EAKLGIVPDS GGVLRLPKIL PPAIVNEMVM TGRRMGAEEA LRWGVVNRVV
     SQAELMDNAR ELAQQLVNSA PLAIAALKEI YRTTSEMPVE EAYRYIRSGV LKNYPSVLHS
     EDAIEGPLAF AEKRDPVWKG R