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P14604

- ECHM_RAT

UniProt

P14604 - ECHM_RAT

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Protein
Enoyl-CoA hydratase, mitochondrial
Gene
Echs1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate.

Catalytic activityi

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei141 – 1411Substrate; via amide nitrogen
Sitei164 – 1641Important for catalytic activity

GO - Molecular functioni

  1. enoyl-CoA hydratase activity Source: RGD

GO - Biological processi

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

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-CoA hydratase, mitochondrial (EC:4.2.1.17)
Alternative name(s):
Enoyl-CoA hydratase 1
Short-chain enoyl-CoA hydratase
Short name:
SCEH
Gene namesi
Name:Echs1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi69330. Echs1.

Subcellular locationi

Mitochondrion matrix 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi144 – 1441E → D: Reduces activity 50-fold. 1 Publication
Mutagenesisi144 – 1441E → Q: Reduces activity 3300-fold. 1 Publication
Mutagenesisi164 – 1641E → D: Reduces activity 1250-fold. 1 Publication
Mutagenesisi164 – 1641E → Q: Reduces activity 330000-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2929Mitochondrion1 Publication
Add
BLAST
Chaini30 – 290261Enoyl-CoA hydratase, mitochondrial
PRO_0000007414Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011N6-acetyllysine; alternate By similarity
Modified residuei101 – 1011N6-succinyllysine; alternate By similarity
Modified residuei115 – 1151N6-acetyllysine; alternate By similarity
Modified residuei115 – 1151N6-succinyllysine; alternate By similarity
Modified residuei204 – 2041N6-succinyllysine By similarity
Modified residuei211 – 2111N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP14604.
PRIDEiP14604.

PTM databases

PhosphoSiteiP14604.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Gene expression databases

GenevestigatoriP14604.

Interactioni

Subunit structurei

Homohexamer; dimer of trimers.3 Publications

Protein-protein interaction databases

IntActiP14604. 1 interaction.
STRINGi10116.ENSRNOP00000025446.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 429
Helixi43 – 453
Beta strandi47 – 526
Helixi55 – 573
Helixi63 – 7816
Beta strandi84 – 885
Beta strandi91 – 955
Helixi100 – 1034
Helixi108 – 1136
Helixi119 – 1257
Beta strandi130 – 1345
Beta strandi136 – 1394
Helixi141 – 1488
Beta strandi149 – 1557
Beta strandi159 – 1613
Helixi163 – 1675
Turni175 – 1773
Helixi178 – 1836
Helixi185 – 19410
Beta strandi197 – 1993
Helixi200 – 2056
Beta strandi210 – 2134
Turni215 – 2173
Helixi218 – 23114
Helixi234 – 24512
Helixi246 – 2483
Helixi252 – 26514
Helixi266 – 2683
Helixi270 – 28011

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DUBX-ray2.50A/B/C/D/E/F30-290[»]
1EY3X-ray2.30A/B/C/D/E/F33-290[»]
1MJ3X-ray2.10A/B/C/D/E/F31-290[»]
2DUBX-ray2.40A/B/C/D/E/F30-290[»]
ProteinModelPortaliP14604.
SMRiP14604. Positions 31-290.

Miscellaneous databases

EvolutionaryTraceiP14604.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1014Substrate binding

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1024.
GeneTreeiENSGT00720000108577.
HOGENOMiHOG000027939.
HOVERGENiHBG010157.
InParanoidiP14604.
KOiK07511.
OMAiHWDQLTR.
OrthoDBiEOG7N63NC.
PhylomeDBiP14604.
TreeFamiTF314497.

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 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.

P14604-1 [UniParc]FASTAAdd to Basket

« Hide

MAALRALLPR ACNSLLSPVR CPEFRRFASG ANFQYIITEK KGKNSSVGLI    50
QLNRPKALNA LCNGLIEELN QALETFEEDP AVGAIVLTGG EKAFAAGADI 100
KEMQNRTFQD CYSGKFLSHW DHITRIKKPV IAAVNGYALG GGCELAMMCD 150
IIYAGEKAQF GQPEILLGTI PGAGGTQRLT RAVGKSLAME MVLTGDRISA 200
QDAKQAGLVS KIFPVETLVE EAIQCAEKIA NNSKIIVAMA KESVNAAFEM 250
TLTEGNKLEK KLFYSTFATD DRREGMSAFV EKRKANFKDH 290
Length:290
Mass (Da):31,516
Last modified:April 1, 1990 - v1
Checksum:i1E528590961D0CC0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X15958 mRNA. Translation: CAA34080.1.
BC064655 mRNA. Translation: AAH64655.1.
PIRiS06477.
RefSeqiNP_511178.1. NM_078623.2.
XP_003748934.1. XM_003748886.2.
UniGeneiRn.6847.

Genome annotation databases

EnsembliENSRNOT00000025446; ENSRNOP00000025446; ENSRNOG00000018522.
ENSRNOT00000071574; ENSRNOP00000066388; ENSRNOG00000047565.
GeneIDi100911186.
140547.
KEGGirno:100911186.
rno:140547.
UCSCiRGD:69330. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X15958 mRNA. Translation: CAA34080.1 .
BC064655 mRNA. Translation: AAH64655.1 .
PIRi S06477.
RefSeqi NP_511178.1. NM_078623.2.
XP_003748934.1. XM_003748886.2.
UniGenei Rn.6847.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DUB X-ray 2.50 A/B/C/D/E/F 30-290 [» ]
1EY3 X-ray 2.30 A/B/C/D/E/F 33-290 [» ]
1MJ3 X-ray 2.10 A/B/C/D/E/F 31-290 [» ]
2DUB X-ray 2.40 A/B/C/D/E/F 30-290 [» ]
ProteinModelPortali P14604.
SMRi P14604. Positions 31-290.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P14604. 1 interaction.
STRINGi 10116.ENSRNOP00000025446.

Chemistry

ChEMBLi CHEMBL3153.

PTM databases

PhosphoSitei P14604.

Proteomic databases

PaxDbi P14604.
PRIDEi P14604.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000025446 ; ENSRNOP00000025446 ; ENSRNOG00000018522 .
ENSRNOT00000071574 ; ENSRNOP00000066388 ; ENSRNOG00000047565 .
GeneIDi 100911186.
140547.
KEGGi rno:100911186.
rno:140547.
UCSCi RGD:69330. rat.

Organism-specific databases

CTDi 1892.
RGDi 69330. Echs1.

Phylogenomic databases

eggNOGi COG1024.
GeneTreei ENSGT00720000108577.
HOGENOMi HOG000027939.
HOVERGENi HBG010157.
InParanoidi P14604.
KOi K07511.
OMAi HWDQLTR.
OrthoDBi EOG7N63NC.
PhylomeDBi P14604.
TreeFami TF314497.

Enzyme and pathway databases

UniPathwayi UPA00659 .

Miscellaneous databases

EvolutionaryTracei P14604.
NextBioi 620493.
PROi P14604.

Gene expression databases

Genevestigatori P14604.

Family and domain databases

Gene3Di 3.90.226.10. 1 hit.
InterProi IPR029045. ClpP/crotonase-like_dom.
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. "Molecular cloning and sequence analysis of the cDNA for rat mitochondrial enoyl-CoA hydratase. Structural and evolutionary relationships linked to the bifunctional enzyme of the peroxisomal beta-oxidation system."
    Minami-Ishii N., Taketani S., Osumi T., Hashimoto T.
    Eur. J. Biochem. 185:73-78(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-39 AND 80-94.
    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: Prostate.
  3. "Enoyl-CoA hydratase and isomerase form a superfamily with a common active-site glutamate residue."
    Mueller-Newen G., Janssen U., Stoffel W.
    Eur. J. Biochem. 228:68-73(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLU-164.
  4. "Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5-A resolution: a spiral fold defines the CoA-binding pocket."
    Engel C.K., Mathieu M., Zeelen J.P., Hiltunen J.K., Wierenga R.K.
    EMBO J. 15:5135-5145(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH OCTANOYL COENZYME A, SUBUNIT.
    Tissue: Liver.
  5. "The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule."
    Engel C.K., Kiema T.R., Hiltunen J.K., Wierenga R.K.
    J. Mol. Biol. 275:847-859(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ACETOACETYL COENZYME A, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Structural mechanism of enoyl-CoA hydratase: three atoms from a single water are added in either an E1cb stepwise or concerted fashion."
    Bahnson B.J., Anderson V.E., Petsko G.A.
    Biochemistry 41:2621-2629(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 33-290 IN COMPLEX WITH 4-N,N-DIMETHYLAMINOCINNAMOYL COENZYME A, ENZYME MECHANISM, SUBUNIT.
  7. "Stereoselectivity of enoyl-CoA hydratase results from preferential activation of one of two bound substrate conformers."
    Bell A.F., Feng Y., Hofstein H.A., Parikh S., Wu J., Rudolph M.J., Kisker C., Whitty A., Tonge P.J.
    Chem. Biol. 9:1247-1255(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 31-290 IN COMPLEX WITH HEXADIENOL COENZYME A, MUTAGENESIS OF GLU-144.

Entry informationi

Entry nameiECHM_RAT
AccessioniPrimary (citable) accession number: P14604
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 11, 2014
This is version 130 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

External Data

Dasty 3

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