CAID_SALEP
ID CAID_SALEP Reviewed; 261 AA.
AC B5R1Q9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 64.
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=SEN0071;
OS Salmonella enteritidis PT4 (strain P125109).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P125109;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(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; AM933172; CAR31660.1; -; Genomic_DNA.
DR RefSeq; WP_000004387.1; NC_011294.1.
DR AlphaFoldDB; B5R1Q9; -.
DR SMR; B5R1Q9; -.
DR KEGG; set:SEN0071; -.
DR HOGENOM; CLU_009834_7_6_6; -.
DR OMA; AMEMIMT; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000000613; 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_1000136262"
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; 28082 MW; 809233D1A3616316 CRC64;
MSESLHLTRN GPILEITLDR PKANAIDAKT SFAMGEAFLN FRDDPELRVA IITGGGEKFF
SAGWDLKAAA EGEAPDADFG SGGFAGLTEI FDLDKPVIAA VNGYAFGGGF ELALAADFIV
CAENASFALP EAKLGIVPDS GGVLRLPKLL PPAIVNEMVM TGRRMSAEEA LRWGVVNRVV
SQSELMDSAR ELAQQLVNSA PLAIAALKEI YRATSEMPVE EGYRYIRSGV LKHYPSVLHS
EDALEGPQAF AEKRDPVWKG R
