CAID_SALTY
ID CAID_SALTY Reviewed; 261 AA.
AC Q8ZRX5;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 105.
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=STM0070;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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 -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_01051, ECO:0000305}.
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DR EMBL; AE006468; AAL19034.1; -; Genomic_DNA.
DR RefSeq; NP_459075.1; NC_003197.2.
DR RefSeq; WP_000004385.1; NC_003197.2.
DR AlphaFoldDB; Q8ZRX5; -.
DR SMR; Q8ZRX5; -.
DR STRING; 99287.STM0070; -.
DR PaxDb; Q8ZRX5; -.
DR EnsemblBacteria; AAL19034; AAL19034; STM0070.
DR GeneID; 1251588; -.
DR KEGG; stm:STM0070; -.
DR PATRIC; fig|99287.12.peg.72; -.
DR HOGENOM; CLU_009834_7_6_6; -.
DR OMA; AMEMIMT; -.
DR PhylomeDB; Q8ZRX5; -.
DR BioCyc; SENT99287:STM0070-MON; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000001014; 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; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..261
FT /note="Carnitinyl-CoA dehydratase"
FT /id="PRO_0000109353"
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; 28106 MW; 11413296E72B4BAF CRC64;
MSESLHLTRN GPILEITLDR PKANAIDAKT SFAMGEAFLN FRDDPELRVA IITGGGEKFF
SAGWDLKAAA EGEAPDADFG PGGFAGLTEI FDLDKPVIAA VNGYAFGGGF ELALAADFIV
CAENASFALP EAKLGIVPDS GGVLRLPKLL PPAIVNEMVM TGRRMSAEEA LRWGVVNRVV
SQSELMESAR ELAQQLVNSA PLAIAALKEI YRATSEMPVE EGYRYIRSGV LKHYPSVLHS
EDALEGPQAF AEKRDPVWKG R
