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Protein

Enoyl-CoA delta isomerase 1, mitochondrial

Gene

Eci1

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

Functioni

Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species.

Catalytic activityi

(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.

Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei140Substrate; via amide nitrogenBy similarity1
Binding sitei164SubstrateBy similarity1
Sitei165Important for catalytic activityBy similarity1

GO - Molecular functioni

  • dodecenoyl-CoA delta-isomerase activity Source: RGD
  • identical protein binding Source: RGD

GO - Biological processi

  • fatty acid beta-oxidation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BRENDAi5.3.3.8. 5301.
SABIO-RKP23965.
UniPathwayiUPA00659.

Chemistry databases

SwissLipidsiSLP:000001593.

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-CoA delta isomerase 1, mitochondrial (EC:5.3.3.8)
Alternative name(s):
3,2-trans-enoyl-CoA isomerase
Delta(3),Delta(2)-enoyl-CoA isomerase
Short name:
D3,D2-enoyl-CoA isomerase
Dodecenoyl-CoA isomerase
Gene namesi
Name:Eci1
Synonyms:Dci
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61892. Eci1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi165E → Q: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 28MitochondrionAdd BLAST28
ChainiPRO_000000742229 – 289Enoyl-CoA delta isomerase 1, mitochondrialAdd BLAST261

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei48N6-acetyllysine; alternateBy similarity1
Modified residuei48N6-succinyllysine; alternateBy similarity1
Modified residuei71N6-succinyllysineBy similarity1
Modified residuei76N6-acetyllysineBy similarity1
Modified residuei222N6-acetyllysine; alternateBy similarity1
Modified residuei222N6-succinyllysine; alternateBy similarity1
Modified residuei229N6-acetyllysine; alternateBy similarity1
Modified residuei229N6-succinyllysine; alternateBy similarity1
Modified residuei255N6-acetyllysine; alternateBy similarity1
Modified residuei255N6-succinyllysine; alternateBy similarity1
Modified residuei275N6-succinyllysineBy similarity1
Modified residuei283N6-acetyllysine; alternateBy similarity1
Modified residuei283N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP23965.
PRIDEiP23965.

PTM databases

iPTMnetiP23965.
PhosphoSitePlusiP23965.

Interactioni

Subunit structurei

Homotrimer.1 Publication

GO - Molecular functioni

  • identical protein binding Source: RGD

Protein-protein interaction databases

IntActiP23965. 1 interactor.
STRINGi10116.ENSRNOP00000011784.

Structurei

Secondary structure

1289
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 37Combined sources6
Beta strandi44 – 49Combined sources6
Turni52 – 55Combined sources4
Helixi59 – 74Combined sources16
Beta strandi80 – 87Combined sources8
Beta strandi89 – 91Combined sources3
Helixi97 – 100Combined sources4
Helixi105 – 123Combined sources19
Beta strandi126 – 133Combined sources8
Beta strandi135 – 138Combined sources4
Helixi139 – 147Combined sources9
Beta strandi148 – 154Combined sources7
Helixi165 – 168Combined sources4
Helixi174 – 184Combined sources11
Helixi186 – 195Combined sources10
Helixi201 – 206Combined sources6
Beta strandi209 – 214Combined sources6
Helixi216 – 218Combined sources3
Helixi219 – 230Combined sources12
Helixi235 – 254Combined sources20
Helixi257 – 269Combined sources13
Helixi271 – 282Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XX4X-ray2.20A29-289[»]
ProteinModelPortaliP23965.
SMRiP23965.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23965.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni93 – 97Substrate bindingBy similarity5

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410ISNQ. Eukaryota.
COG1024. LUCA.
HOVERGENiHBG001112.
InParanoidiP23965.
PhylomeDBiP23965.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
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.

P23965-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALAAARRVL LQAGSRLGRR GAVDGARRFS NKRVLVEKEG EAGIAVMKFK
60 70 80 90 100
NPPVNSLSLE FLTEFVISLE KLENDKSIRG VILTSERPGI FSAGLDLMEM
110 120 130 140 150
YGRNPAHYAE YWKAVQELWL RLYLSNLTLI SAINGASPAG GCLMALTCDY
160 170 180 190 200
RIMADNSKYT IGLNESLLGI VAPFWLKDNY VNTIGHRAAE RALQLGTLFP
210 220 230 240 250
PAEALKVGLV DEVVPEDQVH SKARSVMAKW FTIPDHSRQL TKSMMRKATA
260 270 280
DNLIKQREAD IQNFTSFISR DSIQKSLHVY LEKLKQKKG
Length:289
Mass (Da):32,254
Last modified:March 1, 1992 - v1
Checksum:i79D2CED09DD8FDC6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1 – 8MALAAARR → AGCCAC AA sequence (PubMed:2040594).Curated8
Sequence conflicti260D → N in AAA41073 (PubMed:2040594).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61184 mRNA. Translation: CAA43488.1.
M61112 mRNA. Translation: AAA41073.1.
PIRiS17161.
UniGeneiRn.80835.

Genome annotation databases

UCSCiRGD:61892. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61184 mRNA. Translation: CAA43488.1.
M61112 mRNA. Translation: AAA41073.1.
PIRiS17161.
UniGeneiRn.80835.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XX4X-ray2.20A29-289[»]
ProteinModelPortaliP23965.
SMRiP23965.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP23965. 1 interactor.
STRINGi10116.ENSRNOP00000011784.

Chemistry databases

SwissLipidsiSLP:000001593.

PTM databases

iPTMnetiP23965.
PhosphoSitePlusiP23965.

Proteomic databases

PaxDbiP23965.
PRIDEiP23965.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:61892. rat.

Organism-specific databases

RGDi61892. Eci1.

Phylogenomic databases

eggNOGiENOG410ISNQ. Eukaryota.
COG1024. LUCA.
HOVERGENiHBG001112.
InParanoidiP23965.
PhylomeDBiP23965.

Enzyme and pathway databases

UniPathwayiUPA00659.
BRENDAi5.3.3.8. 5301.
SABIO-RKP23965.

Miscellaneous databases

EvolutionaryTraceiP23965.
PROiP23965.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
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 nameiECI1_RAT
AccessioniPrimary (citable) accession number: P23965
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: November 2, 2016
This is version 122 of the entry and version 1 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

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.