ID   CAID_ECOLC              Reviewed;         261 AA.
AC   B1IRE0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
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}; OrderedLocusNames=EcolC_3619;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000946; ACA79233.1; -; Genomic_DNA.
DR   RefSeq; WP_001295419.1; NZ_CP022959.1.
DR   AlphaFoldDB; B1IRE0; -.
DR   SMR; B1IRE0; -.
DR   GeneID; 58460825; -.
DR   KEGG; ecl:EcolC_3619; -.
DR   HOGENOM; CLU_009834_7_6_6; -.
DR   OMA; AMEMIMT; -.
DR   UniPathway; UPA00117; -.
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_1000084425"
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;  28190 MW;  2C4DD6C3D16995CC CRC64;
     MSESLHLTRN GSILEITLDR PKANAIDAKT SFEMGEVFLN FRDDPQLRVA IITGAGEKFF
     SAGWDLKAAA EGEAPDADFG PGGFAGLTEI FNLDKPVIAA VNGYAFGGGF ELALAADFIV
     CADNASFALP EAKLGIVPDS GGVLRLPKIL PPAIVNEMVM TGRRMGAEEA LRWGIVNRVV
     SQAELMDNAR ELAQQLVNSA PLAIAALKEI YRTTSEMPVE EAYRYIRSGV LKHYPSVLHS
     EDAIEGPLAF AEKRDPVWKG R