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Q62651

- ECH1_RAT

UniProt

Q62651 - ECH1_RAT

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Protein

Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial

Gene

Ech1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei173 – 1731Substrate; via amide nitrogenBy similarity
Sitei196 – 1961Important for catalytic activityCurated
Sitei204 – 2041Important for catalytic activitySequence Analysis

GO - Molecular functioni

  1. isomerase activity Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. fatty acid beta-oxidation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial (EC:5.3.3.-)
Gene namesi
Name:Ech1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi69353. Ech1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. mitochondrion Source: UniProtKB
  3. peroxisome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionSequence AnalysisAdd
BLAST
Chaini34 – 327294Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrialPRO_0000007419Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei230 – 2301N6-succinyllysineBy similarity
Modified residuei316 – 3161N6-succinyllysineBy similarity
Modified residuei326 – 3261N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ62651.
PRIDEiQ62651.

Expressioni

Gene expression databases

GenevestigatoriQ62651.

Interactioni

Subunit structurei

Homohexamer.1 Publication

Protein-protein interaction databases

IntActiQ62651. 1 interaction.
MINTiMINT-4597589.
STRINGi10116.ENSRNOP00000027537.

Structurei

Secondary structure

1
327
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi55 – 639
Beta strandi66 – 716
Helixi74 – 763
Helixi82 – 9615
Beta strandi103 – 1097
Helixi119 – 1268
Helixi134 – 15724
Beta strandi158 – 1603
Beta strandi162 – 1665
Beta strandi168 – 1714
Helixi173 – 1786
Beta strandi181 – 1877
Beta strandi191 – 1933
Helixi196 – 1994
Helixi207 – 2104
Helixi211 – 2133
Helixi218 – 22710
Beta strandi230 – 2323
Helixi233 – 2386
Beta strandi241 – 2488
Helixi249 – 26517
Helixi268 – 28316
Helixi286 – 30015
Helixi304 – 31411
Helixi319 – 3213

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DCIX-ray1.50A/B/C54-327[»]
ProteinModelPortaliQ62651.
SMRiQ62651. Positions 54-327.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ62651.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi325 – 3273Microbody targeting signalSequence Analysis

Sequence similaritiesi

Keywords - Domaini

Transit peptide, Zinc-finger

Phylogenomic databases

eggNOGiCOG1024.
GeneTreeiENSGT00760000119100.
HOGENOMiHOG000027939.
HOVERGENiHBG005556.
InParanoidiQ62651.
KOiK12663.
OMAiSWVKDVC.
OrthoDBiEOG7JHM64.
PhylomeDBiQ62651.
TreeFamiTF314317.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamiPF00378. ECH. 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.

Q62651 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATAMTVSSK LLGLLMQQLR GTRQLYFNVS LRSLSSSAQE ASKRIPEEVS
60 70 80 90 100
DHNYESIQVT SAQKHVLHVQ LNRPEKRNAM NRAFWRELVE CFQKISKDSD
110 120 130 140 150
CRAVVVSGAG KMFTSGIDLM DMASDILQPP GDDVARIAWY LRDLISRYQK
160 170 180 190 200
TFTVIEKCPK PVIAAIHGGC IGGGVDLISA CDIRYCTQDA FFQVKEVDVG
210 220 230 240 250
LAADVGTLQR LPKVIGNRSL VNELTFTARK MMADEALDSG LVSRVFPDKD
260 270 280 290 300
VMLNAAFALA ADISSKSPVA VQGSKINLIY SRDHSVDESL DYMATWNMSM
310 320
LQTQDIIKSV QAAMEKKDSK SITFSKL
Length:327
Mass (Da):36,172
Last modified:July 15, 1999 - v2
Checksum:i6FAE35D7D5F66BC2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti164 – 1641A → T in AAA82008. (PubMed:7558027)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U08976 mRNA. Translation: AAA82008.1.
BC062226 mRNA. Translation: AAH62226.1.
PIRiA57626.
RefSeqiNP_072116.1. NM_022594.1.
UniGeneiRn.6148.

Genome annotation databases

EnsembliENSRNOT00000027537; ENSRNOP00000027537; ENSRNOG00000020308.
GeneIDi64526.
KEGGirno:64526.
UCSCiRGD:69353. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U08976 mRNA. Translation: AAA82008.1 .
BC062226 mRNA. Translation: AAH62226.1 .
PIRi A57626.
RefSeqi NP_072116.1. NM_022594.1.
UniGenei Rn.6148.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DCI X-ray 1.50 A/B/C 54-327 [» ]
ProteinModelPortali Q62651.
SMRi Q62651. Positions 54-327.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q62651. 1 interaction.
MINTi MINT-4597589.
STRINGi 10116.ENSRNOP00000027537.

Proteomic databases

PaxDbi Q62651.
PRIDEi Q62651.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000027537 ; ENSRNOP00000027537 ; ENSRNOG00000020308 .
GeneIDi 64526.
KEGGi rno:64526.
UCSCi RGD:69353. rat.

Organism-specific databases

CTDi 1891.
RGDi 69353. Ech1.

Phylogenomic databases

eggNOGi COG1024.
GeneTreei ENSGT00760000119100.
HOGENOMi HOG000027939.
HOVERGENi HBG005556.
InParanoidi Q62651.
KOi K12663.
OMAi SWVKDVC.
OrthoDBi EOG7JHM64.
PhylomeDBi Q62651.
TreeFami TF314317.

Enzyme and pathway databases

UniPathwayi UPA00659 .

Miscellaneous databases

EvolutionaryTracei Q62651.
NextBioi 613350.
PROi Q62651.

Gene expression databases

Genevestigatori Q62651.

Family and domain databases

Gene3Di 1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProi IPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view ]
Pfami PF00378. ECH. 1 hit.
[Graphical view ]
SUPFAMi SSF52096. SSF52096. 1 hit.
PROSITEi PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of rat and human cDNAs encoding a novel putative peroxisomal enoyl-CoA hydratase."
    Fitzpatrick D.R., Germain-Lee E., Valle D.
    Genomics 27:457-466(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary.
  3. Lubec G., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 185-210 AND 219-229, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.
  4. "Delta3,5-delta2,4-dienoyl-CoA isomerase from rat liver. Molecular characterization."
    Filppula S.A., Yagi A.I., Kilpeleainen S.H., Novikov D., Fitzpatrick D.R., Vihinen M., Valle D., Hiltunen J.K.
    J. Biol. Chem. 273:349-355(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Tissue: Liver.
  5. "The crystal structure of dienoyl-CoA isomerase at 1.5 A resolution reveals the importance of aspartate and glutamate sidechains for catalysis."
    Modis Y., Filppula S.A., Novikov D.K., Norledge B., Hiltunen J.K., Wierenga R.K.
    Structure 6:957-970(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), SEQUENCE REVISION TO 164, SUBUNIT.

Entry informationi

Entry nameiECH1_RAT
AccessioniPrimary (citable) accession number: Q62651
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1999
Last modified: October 29, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3