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Protein

Carnitinyl-CoA dehydratase

Gene

caiD

Organism
Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)
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)LengthDescriptionGraphical viewFeature identifierActions
Sitei111 – 1111Important for catalytic activityUniRule annotation
Sitei131 – 1311Important for catalytic activityUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

BioCyciCKOS290338:GJ8L-3340-MONOMER.
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:CKO_03347
OrganismiCitrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)
Taxonomic identifieri290338 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacter
Proteomesi
  • UP000008148 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Carnitinyl-CoA dehydratasePRO_1000064340Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi290338.CKO_03347.

Structurei

3D structure databases

ProteinModelPortaliA8ALR7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105E39. Bacteria.
COG1024. LUCA.
HOGENOMiHOG000027939.
KOiK08299.
OMAiMAAHFRI.
OrthoDBiPOG091H01K6.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
HAMAPiMF_01051. CaiD. 1 hit.
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.

A8ALR7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSESLHFTRH GPILEITLDR PKANAIDAKT SFEMGEVFLN FRDDPELRVA
60 70 80 90 100
IITGGGEKFF SAGWDLKAAA EGEAPDADFG PGGFAGLTEI FDLDKPVIAA
110 120 130 140 150
VNGYAFGGGF ELALAADFIV CADNASFALP EAKLGIVPDS GGVLRLPKLL
160 170 180 190 200
PPAIVNEMLM TGRRMDAEEA LRWGIVNRVV SQQALMDSAR ELAQQLVNSA
210 220 230 240 250
PLAIAALKEI YRATSEMPVE EGYRYIRSGA LKHYPSVLHS EDAIEGPQAF
260
AEKRDPVWKG R
Length:261
Mass (Da):28,232
Last modified:October 23, 2007 - v1
Checksum:i503DF8B6644036CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000822 Genomic DNA. Translation: ABV14430.1.
RefSeqiWP_012134133.1. NC_009792.1.

Genome annotation databases

EnsemblBacteriaiABV14430; ABV14430; CKO_03347.
KEGGicko:CKO_03347.
PATRICi20389260. VBICitKos71230_2808.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000822 Genomic DNA. Translation: ABV14430.1.
RefSeqiWP_012134133.1. NC_009792.1.

3D structure databases

ProteinModelPortaliA8ALR7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi290338.CKO_03347.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV14430; ABV14430; CKO_03347.
KEGGicko:CKO_03347.
PATRICi20389260. VBICitKos71230_2808.

Phylogenomic databases

eggNOGiENOG4105E39. Bacteria.
COG1024. LUCA.
HOGENOMiHOG000027939.
KOiK08299.
OMAiMAAHFRI.
OrthoDBiPOG091H01K6.

Enzyme and pathway databases

UniPathwayiUPA00117.
BioCyciCKOS290338:GJ8L-3340-MONOMER.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
HAMAPiMF_01051. CaiD. 1 hit.
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...

Entry informationi

Entry nameiCAID_CITK8
AccessioniPrimary (citable) accession number: A8ALR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: September 7, 2016
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.