CAID_ECOL5
ID CAID_ECOL5 Reviewed; 261 AA.
AC Q0TLV3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=ECP_0036;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG68078.1; -; Genomic_DNA.
DR RefSeq; WP_000004399.1; NC_008253.1.
DR AlphaFoldDB; Q0TLV3; -.
DR SMR; Q0TLV3; -.
DR STRING; 362663.ECP_0036; -.
DR EnsemblBacteria; ABG68078; ABG68078; ECP_0036.
DR KEGG; ecp:ECP_0036; -.
DR HOGENOM; CLU_009834_7_6_6; -.
DR OMA; AMEMIMT; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000009182; 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_1000064341"
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; 28176 MW; D2BC39DD3E6983B6 CRC64;
MSESLHLTRN GSILEITLDR PKANAIDAKT SFEMGEVFLN FRDDPQLRVA IITGAGEKFF
SAGWDLKAAA EGEAPDADFG PGGFAGLTEI FNLDKPVIAA VNGYAFGGGF ELALAADFIV
CADNASFALP EAKLGIVPDS GGVLRLPKIL PPAIVNEMVM TGRRMGAEEA LRWGVVNRVV
SQAELMDNAR ELAQQLVNSA PLAIAALKEI YRTTSEMPVE EAYRYIRSGV LKHYPSVLHS
EDAIEGPLAF AEKRDPVWKG R