ID   CAID_PROSL              Reviewed;         261 AA.
AC   Q8GB17;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 70.
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};
OS   Proteus sp. (strain LE138).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=217617;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Engemann C., Elssner T., Pfeifer S., Krumbholz C., Maier T., Kleber H.-P.;
RT   "Cai locus and corresponding enzymes of Proteus sp.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-21, AND SUBUNIT.
RX   PubMed=11409545; DOI=10.1007/s002030100272;
RA   Engemann C., Elssner T., Kleber H.-P.;
RT   "Biotransformation of crotonobetaine to L(-)-carnitine in Proteus sp.";
RL   Arch. Microbiol. 175:353-359(2001).
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   -!- SUBUNIT: Homotrimer. {ECO:0000305|PubMed:11409545}.
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; AJ508908; CAD48582.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8GB17; -.
DR   SMR; Q8GB17; -.
DR   KEGG; ag:CAD48582; -.
DR   BRENDA; 4.2.1.149; 5048.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Lyase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11409545"
FT   CHAIN           2..261
FT                   /note="Carnitinyl-CoA dehydratase"
FT                   /id="PRO_0000109351"
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;  28184 MW;  87BF6AE0A553FE43 CRC64;
     MSQSLHLTTR GSVLEIILDR PKANAIDAKT SHEMGEVFMR FRDDPSLRVA IITGAGERFF
     CAGWDLKAAA EGEAPDADFG AGGFAGLTEL FDLNKPVIAA INGYAFGGGF ELALAADMII
     CSDNASFALP EAQLGIVPDS GGVLRLPKRL PPAIVNEMLM TGRRMNAQEA LRWGIANRVV
     SATELMDSAR ELADQIANSA PLAVAALKEI YRATSELSIE EGYKLMRSGV LKYYPRVLHS
     EDALEGPLAF AEKRSPEWKG R