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Protein

Carnitinyl-CoA dehydratase

Gene

caiD

Organism
Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the reversible dehydration of L-carnitinyl-CoA to crotonobetainyl-CoA.UniRule annotation

Catalytic activityi

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

Pathwayi: carnitine metabolism

This protein is involved in the pathway carnitine metabolism, which is part of Amine and polyamine metabolism.UniRule annotation
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)DescriptionActionsGraphical viewLength
Sitei111Important for catalytic activityUniRule annotation1
Sitei131Important for catalytic activityUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase

Enzyme and pathway databases

UniPathwayiUPA00117.

Names & Taxonomyi

Protein namesi
Recommended name:
Carnitinyl-CoA dehydrataseUniRule annotation (EC:4.2.1.149UniRule annotation)
Alternative name(s):
Crotonobetainyl-CoA hydrataseUniRule annotation
Gene namesi
Name:caiDUniRule annotation
Ordered Locus Names:EcolC_3619
OrganismiEscherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)
Taxonomic identifieri481805 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000844251 – 261Carnitinyl-CoA dehydrataseAdd BLAST261

Structurei

3D structure databases

ProteinModelPortaliB1IRE0.
SMRiB1IRE0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the enoyl-CoA hydratase/isomerase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4106YT9. Bacteria.
COG1024. LUCA.
HOGENOMiHOG000027939.
KOiK08299.
OMAiKGRAMEM.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
HAMAPiMF_01051. CaiD. 1 hit.
InterProiView protein in InterPro
IPR022852. Carnitinyl_CoA_dehydratase.
IPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
PfamiView protein in Pfam
PF00378. ECH_1. 1 hit.
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiView protein in PROSITE
PS00166. ENOYL_COA_HYDRATASE. 1 hit.

Sequencei

Sequence statusi: Complete.

B1IRE0-1 [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:April 29, 2008 - v1
Checksum:i2C4DD6C3D16995CC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000946 Genomic DNA. Translation: ACA79233.1.
RefSeqiWP_001295419.1. NC_010468.1.

Genome annotation databases

EnsemblBacteriaiACA79233; ACA79233; EcolC_3619.
KEGGiecl:EcolC_3619.

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.

Entry informationi

Entry nameiCAID_ECOLC
AccessioniPrimary (citable) accession number: B1IRE0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 29, 2008
Last modified: July 5, 2017
This is version 57 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families