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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei140 – 1401Substrate; via amide nitrogenBy similarity
Binding sitei164 – 1641SubstrateBy similarity
Sitei165 – 1651Important for catalytic activityBy similarity

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi165 – 1651E → Q: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828MitochondrionAdd
BLAST
Chaini29 – 289261Enoyl-CoA delta isomerase 1, mitochondrialPRO_0000007422Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481N6-acetyllysine; alternateBy similarity
Modified residuei48 – 481N6-succinyllysine; alternateBy similarity
Modified residuei71 – 711N6-succinyllysineBy similarity
Modified residuei76 – 761N6-acetyllysineBy similarity
Modified residuei222 – 2221N6-acetyllysine; alternateBy similarity
Modified residuei222 – 2221N6-succinyllysine; alternateBy similarity
Modified residuei229 – 2291N6-acetyllysine; alternateBy similarity
Modified residuei229 – 2291N6-succinyllysine; alternateBy similarity
Modified residuei255 – 2551N6-acetyllysine; alternateBy similarity
Modified residuei255 – 2551N6-succinyllysine; alternateBy similarity
Modified residuei275 – 2751N6-succinyllysineBy similarity
Modified residuei283 – 2831N6-acetyllysine; alternateBy similarity
Modified residuei283 – 2831N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP23965.
PRIDEiP23965.

PTM databases

iPTMnetiP23965.
PhosphoSiteiP23965.

Interactioni

Subunit structurei

Homotrimer.1 Publication

GO - Molecular functioni

  • identical protein binding Source: RGD

Protein-protein interaction databases

IntActiP23965. 1 interaction.
STRINGi10116.ENSRNOP00000011784.

Structurei

Secondary structure

1
289
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 376Combined sources
Beta strandi44 – 496Combined sources
Turni52 – 554Combined sources
Helixi59 – 7416Combined sources
Beta strandi80 – 878Combined sources
Beta strandi89 – 913Combined sources
Helixi97 – 1004Combined sources
Helixi105 – 12319Combined sources
Beta strandi126 – 1338Combined sources
Beta strandi135 – 1384Combined sources
Helixi139 – 1479Combined sources
Beta strandi148 – 1547Combined sources
Helixi165 – 1684Combined sources
Helixi174 – 18411Combined sources
Helixi186 – 19510Combined sources
Helixi201 – 2066Combined sources
Beta strandi209 – 2146Combined sources
Helixi216 – 2183Combined sources
Helixi219 – 23012Combined sources
Helixi235 – 25420Combined sources
Helixi257 – 26913Combined sources
Helixi271 – 28212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XX4X-ray2.20A29-289[»]
ProteinModelPortaliP23965.
SMRiP23965. Positions 29-285.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23965.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni93 – 975Substrate bindingBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 88MALAAARR → AGCCAC AA sequence (PubMed:2040594).Curated
Sequence conflicti260 – 2601D → N in AAA41073 (PubMed:2040594).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1XX4X-ray2.20A29-289[»]
ProteinModelPortaliP23965.
SMRiP23965. Positions 29-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP23965. 1 interaction.
STRINGi10116.ENSRNOP00000011784.

PTM databases

iPTMnetiP23965.
PhosphoSiteiP23965.

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...

Publicationsi

  1. "Mitochondrial 3-2trans-Enoyl-CoA isomerase. Purification, cloning, expression, and mitochondrial import of the key enzyme of unsaturated fatty acid beta-oxidation."
    Mueller-Newen G., Stoffel W.
    Biol. Chem. Hoppe-Seyler 372:613-624(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  2. "Amino acid sequence similarities of the mitochondrial short chain delta 3, delta 2-enoyl-CoA isomerase and peroxisomal multifunctional delta 3, delta 2-enoyl-CoA isomerase, 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase enzyme in rat liver. The proposed occurrence of isomerization and hydration in the same catalytic domain of the multifunctional enzyme."
    Palosaari P.M., Vihinen M., Maentsaelae P.I., Alexson S.E., Pihlajaniemi T., Hiltunen J.K.
    J. Biol. Chem. 266:10750-10753(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  3. "Site-directed mutagenesis of putative active-site amino acid residues of 3,2-trans-enoyl-CoA isomerase, conserved within the low-homology isomerase/hydratase enzyme family."
    Mueller-Newen G., Stoffel W.
    Biochemistry 32:11405-11412(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLU-165.
  4. "Domain swapping in the low-similarity isomerase/hydratase superfamily: the crystal structure of rat mitochondrial delta3, delta2-enoyl-CoA isomerase."
    Hubbard P.A., Yu W., Schulz H., Kim J.-J.P.
    Protein Sci. 14:1545-1555(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 29-289, SUBUNIT.

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: February 17, 2016
This is version 119 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.