CAID_ECOLI
ID CAID_ECOLI Reviewed; 261 AA.
AC P31551; P75623;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Carnitinyl-CoA dehydratase {ECO:0000255|HAMAP-Rule:MF_01051, ECO:0000305};
DE EC=4.2.1.149 {ECO:0000255|HAMAP-Rule:MF_01051, ECO:0000269|PubMed:11551212};
DE AltName: Full=Crotonobetainyl-CoA hydratase {ECO:0000255|HAMAP-Rule:MF_01051, ECO:0000303|PubMed:11551212};
GN Name=caiD {ECO:0000255|HAMAP-Rule:MF_01051, ECO:0000303|PubMed:7815937};
GN Synonyms=yaaL; OrderedLocusNames=b0036, JW0035;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=O44:K74;
RX PubMed=7815937; DOI=10.1111/j.1365-2958.1994.tb00470.x;
RA Eichler K., Bourgis F., Buchet A., Kleber H.-P., Mandrand-Berthelot M.-A.;
RT "Molecular characterization of the cai operon necessary for carnitine
RT metabolism in Escherichia coli.";
RL Mol. Microbiol. 13:775-786(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 108.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=O44:K74;
RX PubMed=11551212; DOI=10.1021/bi0108812;
RA Elssner T., Engemann C., Baumgart K., Kleber H.-P.;
RT "Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA
RT hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-
RT carnitine by Escherichia coli.";
RL Biochemistry 40:11140-11148(2001).
CC -!- FUNCTION: Catalyzes the reversible dehydration of L-carnitinyl-CoA to
CC crotonobetainyl-CoA (PubMed:11551212). Can also hydrate crotonyl-CoA to
CC hydroxybutyryl-CoA (PubMed:11551212). {ECO:0000269|PubMed:11551212}.
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, ECO:0000269|PubMed:11551212};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:45584, ChEBI:CHEBI:15377, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:78611; Evidence={ECO:0000269|PubMed:11551212};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12 uM for crotonobetainyl-CoA {ECO:0000269|PubMed:11551212};
CC KM=38 uM for crotonyl-CoA {ECO:0000269|PubMed:11551212};
CC Vmax=186 umol/min/mg enzyme with crotonobetainyl-CoA as substrate
CC {ECO:0000269|PubMed:11551212};
CC Vmax=0.3 umol/min/mg enzyme with crotonyl-CoA as substrate
CC {ECO:0000269|PubMed:11551212};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_01051}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:11551212}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_01051, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB96605.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA52114.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X73904; CAA52114.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73147.2; -; Genomic_DNA.
DR EMBL; AP009048; BAB96605.2; ALT_INIT; Genomic_DNA.
DR PIR; D64724; D64724.
DR RefSeq; NP_414578.2; NC_000913.3.
DR RefSeq; WP_001295419.1; NZ_LN832404.1.
DR AlphaFoldDB; P31551; -.
DR SMR; P31551; -.
DR BioGRID; 4261692; 569.
DR BioGRID; 853243; 1.
DR IntAct; P31551; 9.
DR STRING; 511145.b0036; -.
DR jPOST; P31551; -.
DR PaxDb; P31551; -.
DR PRIDE; P31551; -.
DR EnsemblBacteria; AAC73147; AAC73147; b0036.
DR EnsemblBacteria; BAB96605; BAB96605; BAB96605.
DR GeneID; 58460825; -.
DR GeneID; 948995; -.
DR KEGG; ecj:JW0035; -.
DR KEGG; eco:b0036; -.
DR PATRIC; fig|1411691.4.peg.2247; -.
DR EchoBASE; EB1518; -.
DR eggNOG; COG1024; Bacteria.
DR HOGENOM; CLU_009834_7_6_6; -.
DR InParanoid; P31551; -.
DR OMA; AMEMIMT; -.
DR PhylomeDB; P31551; -.
DR BioCyc; EcoCyc:CARNRACE-MON; -.
DR BioCyc; MetaCyc:CARNRACE-MON; -.
DR BRENDA; 4.2.1.149; 2026.
DR SABIO-RK; P31551; -.
DR UniPathway; UPA00117; -.
DR PRO; PR:P31551; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008809; F:carnitine racemase activity; EXP:EcoliWiki.
DR GO; GO:0120092; F:crotonyl-CoA hydratase activity; IEA:RHEA.
DR GO; GO:0042413; P:carnitine catabolic process; EXP:EcoliWiki.
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; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11551212"
FT CHAIN 2..261
FT /note="Carnitinyl-CoA dehydratase"
FT /id="PRO_0000109348"
FT ACT_SITE 111
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q5LLW6, ECO:0000255|HAMAP-
FT Rule:MF_01051"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q5LLW6, ECO:0000255|HAMAP-
FT Rule:MF_01051"
FT VARIANT 247
FT /note="P -> L (in strain: O44:K74)"
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
