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Protein

Carnitinyl-CoA dehydratase

Gene

caiD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible dehydration of L-carnitinyl-CoA to crotonobetainyl-CoA.1 Publication

Catalytic activityi

L-carnitinyl-CoA = (E)-4-(trimethylammonio)but-2-enoyl-CoA + H2O.1 Publication

Kineticsi

  1. KM=12 µM for crotonobetainyl-CoA1 Publication
  2. KM=38 µM for crotonyl-CoA1 Publication
  1. Vmax=186 µmol/min/mg enzyme with crotonobetainyl-CoA as substrate1 Publication
  2. Vmax=0.3 µmol/min/mg enzyme with crotonyl-CoA as substrate1 Publication

Pathwayi: carnitine metabolism

This protein is involved in the pathway carnitine metabolism, which is part of Amine and polyamine metabolism.
View all proteins of this organism that are known to be involved in the pathway carnitine metabolism and in Amine and polyamine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei111 – 1111Important for catalytic activityBy similarity
Sitei131 – 1311Important for catalytic activityBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

BioCyciEcoCyc:CARNRACE-MONOMER.
ECOL316407:JW0035-MONOMER.
MetaCyc:CARNRACE-MONOMER.
BRENDAi4.2.1.149. 2026.
UniPathwayiUPA00117.

Names & Taxonomyi

Protein namesi
Recommended name:
Carnitinyl-CoA dehydratase (EC:4.2.1.149)
Alternative name(s):
Crotonobetainyl-CoA hydratase
Gene namesi
Name:caiD
Synonyms:yaaL
Ordered Locus Names:b0036, JW0035
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11557. caiD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 261260Carnitinyl-CoA dehydratasePRO_0000109348Add
BLAST

Proteomic databases

PaxDbiP31551.
PRIDEiP31551.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

BioGridi4261692. 569 interactions.
IntActiP31551. 9 interactions.
STRINGi511145.b0036.

Structurei

3D structure databases

ProteinModelPortaliP31551.
SMRiP31551. Positions 9-261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4106YT9. Bacteria.
COG1024. LUCA.
HOGENOMiHOG000027939.
InParanoidiP31551.
KOiK08299.
OMAiMAAHFRI.
OrthoDBiEOG6M9F0M.
PhylomeDBiP31551.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
HAMAPiMF_01051. CaiD.
InterProiIPR022852. Carnitinyl_CoA_dehydratase.
IPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamiPF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31551-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSESLHLTRN GSILEITLDR PKANAIDAKT SFEMGEVFLN FRDDPQLRVA
60 70 80 90 100
IITGAGEKFF SAGWDLKAAA EGEAPDADFG PGGFAGLTEI FNLDKPVIAA
110 120 130 140 150
VNGYAFGGGF ELALAADFIV CADNASFALP EAKLGIVPDS GGVLRLPKIL
160 170 180 190 200
PPAIVNEMVM TGRRMGAEEA LRWGIVNRVV SQAELMDNAR ELAQQLVNSA
210 220 230 240 250
PLAIAALKEI YRTTSEMPVE EAYRYIRSGV LKHYPSVLHS EDAIEGPLAF
260
AEKRDPVWKG R
Length:261
Mass (Da):28,190
Last modified:January 23, 2007 - v4
Checksum:i2C4DD6C3D16995CC
GO

Sequence cautioni

The sequence BAB96605.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA52114.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti247 – 2471P → L in strain: O44:K74.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73904 Genomic DNA. Translation: CAA52114.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73147.2.
AP009048 Genomic DNA. Translation: BAB96605.2. Different initiation.
PIRiD64724.
RefSeqiNP_414578.2. NC_000913.3.
WP_001295419.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73147; AAC73147; b0036.
BAB96605; BAB96605; BAB96605.
GeneIDi948995.
KEGGiecj:JW0035.
eco:b0036.
PATRICi32115167. VBIEscCol129921_0035.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73904 Genomic DNA. Translation: CAA52114.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73147.2.
AP009048 Genomic DNA. Translation: BAB96605.2. Different initiation.
PIRiD64724.
RefSeqiNP_414578.2. NC_000913.3.
WP_001295419.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP31551.
SMRiP31551. Positions 9-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261692. 569 interactions.
IntActiP31551. 9 interactions.
STRINGi511145.b0036.

Proteomic databases

PaxDbiP31551.
PRIDEiP31551.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73147; AAC73147; b0036.
BAB96605; BAB96605; BAB96605.
GeneIDi948995.
KEGGiecj:JW0035.
eco:b0036.
PATRICi32115167. VBIEscCol129921_0035.

Organism-specific databases

EchoBASEiEB1518.
EcoGeneiEG11557. caiD.

Phylogenomic databases

eggNOGiENOG4106YT9. Bacteria.
COG1024. LUCA.
HOGENOMiHOG000027939.
InParanoidiP31551.
KOiK08299.
OMAiMAAHFRI.
OrthoDBiEOG6M9F0M.
PhylomeDBiP31551.

Enzyme and pathway databases

UniPathwayiUPA00117.
BioCyciEcoCyc:CARNRACE-MONOMER.
ECOL316407:JW0035-MONOMER.
MetaCyc:CARNRACE-MONOMER.
BRENDAi4.2.1.149. 2026.

Miscellaneous databases

PROiP31551.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
HAMAPiMF_01051. CaiD.
InterProiIPR022852. Carnitinyl_CoA_dehydratase.
IPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamiPF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli."
    Eichler K., Bourgis F., Buchet A., Kleber H.-P., Mandrand-Berthelot M.-A.
    Mol. Microbiol. 13:775-786(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: O44:K74.
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
    Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
    Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 108.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli."
    Elssner T., Engemann C., Baumgart K., Kleber H.-P.
    Biochemistry 40:11140-11148(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: O44:K74.

Entry informationi

Entry nameiCAID_ECOLI
AccessioniPrimary (citable) accession number: P31551
Secondary accession number(s): P75623
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 136 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.