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Protein

Enoyl-CoA hydratase, mitochondrial

Gene

Echs1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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. Has high substrate specificity for crotonyl-CoA and moderate specificity for acryloyl-CoA, 3-methylcrotonyl-CoA and methacrylyl-CoA. It is noteworthy that binds tiglyl-CoA, but hydrates only a small amount of this substrate.By similarity

Catalytic activityi

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

Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.By similarity
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 sitei141Substrate; via amide nitrogen1
Sitei164Important for catalytic activity1

GO - Molecular functioni

  • enoyl-CoA hydratase activity Source: RGD

GO - Biological processi

  • fatty acid beta-oxidation Source: RGD

Keywordsi

Molecular functionLyase
Biological processFatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BRENDAi4.2.1.17 5301
ReactomeiR-RNO-77310 Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA
R-RNO-77346 Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA
R-RNO-77348 Beta oxidation of octanoyl-CoA to hexanoyl-CoA
R-RNO-77350 Beta oxidation of hexanoyl-CoA to butanoyl-CoA
R-RNO-77352 Beta oxidation of butanoyl-CoA to acetyl-CoA
UniPathwayiUPA00659

Chemistry databases

SwissLipidsiSLP:000001128

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-CoA hydratase, mitochondrial (EC:4.2.1.17By similarity)
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi69330 Echs1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi144E → D: Reduces activity 50-fold. 1 Publication1
Mutagenesisi144E → Q: Reduces activity 3300-fold. 1 Publication1
Mutagenesisi164E → D: Reduces activity 1250-fold. 1 Publication1
Mutagenesisi164E → Q: Reduces activity 330000-fold. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3153

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 29Mitochondrion1 PublicationAdd BLAST29
ChainiPRO_000000741430 – 290Enoyl-CoA hydratase, mitochondrialAdd BLAST261

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei101N6-acetyllysine; alternateBy similarity1
Modified residuei101N6-succinyllysine; alternateBy similarity1
Modified residuei115N6-acetyllysine; alternateBy similarity1
Modified residuei115N6-succinyllysine; alternateBy similarity1
Modified residuei204N6-succinyllysineBy similarity1
Modified residuei211N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP14604
PRIDEiP14604

PTM databases

iPTMnetiP14604
PhosphoSitePlusiP14604

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Gene expression databases

BgeeiENSRNOG00000018522
GenevisibleiP14604 RN

Interactioni

Subunit structurei

Homohexamer; dimer of trimers.4 Publications

Protein-protein interaction databases

IntActiP14604, 1 interactor
STRINGi10116.ENSRNOP00000066388

Structurei

Secondary structure

1290
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 42Combined sources9
Helixi43 – 45Combined sources3
Beta strandi47 – 52Combined sources6
Helixi55 – 57Combined sources3
Helixi63 – 78Combined sources16
Beta strandi84 – 88Combined sources5
Beta strandi91 – 95Combined sources5
Helixi100 – 103Combined sources4
Helixi108 – 113Combined sources6
Helixi119 – 125Combined sources7
Beta strandi130 – 134Combined sources5
Beta strandi136 – 139Combined sources4
Helixi141 – 148Combined sources8
Beta strandi149 – 155Combined sources7
Beta strandi159 – 161Combined sources3
Helixi163 – 167Combined sources5
Turni175 – 177Combined sources3
Helixi178 – 183Combined sources6
Helixi185 – 194Combined sources10
Beta strandi197 – 199Combined sources3
Helixi200 – 205Combined sources6
Beta strandi210 – 213Combined sources4
Turni215 – 217Combined sources3
Helixi218 – 231Combined sources14
Helixi234 – 245Combined sources12
Helixi246 – 248Combined sources3
Helixi252 – 265Combined sources14
Helixi266 – 268Combined sources3
Helixi270 – 280Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14604

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni98 – 101Substrate binding4

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1680 Eukaryota
COG1024 LUCA
GeneTreeiENSGT00890000139344
HOGENOMiHOG000027939
HOVERGENiHBG010157
InParanoidiP14604
KOiK07511
OMAiIFKQTDA
OrthoDBiEOG091G0MVQ
PhylomeDBiP14604
TreeFamiTF314497

Family and domain databases

Gene3Di1.10.12.10, 1 hit
InterProiView protein in InterPro
IPR029045 ClpP/crotonase-like_dom_sf
IPR018376 Enoyl-CoA_hyd/isom_CS
IPR001753 Enoyl-CoA_hydra/iso
IPR014748 enoyl-CoA_hydra_C
PfamiView protein in Pfam
PF00378 ECH_1, 1 hit
SUPFAMiSSF52096 SSF52096, 1 hit
PROSITEiView protein in PROSITE
PS00166 ENOYL_COA_HYDRATASE, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14604-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALRALLPR ACNSLLSPVR CPEFRRFASG ANFQYIITEK KGKNSSVGLI
60 70 80 90 100
QLNRPKALNA LCNGLIEELN QALETFEEDP AVGAIVLTGG EKAFAAGADI
110 120 130 140 150
KEMQNRTFQD CYSGKFLSHW DHITRIKKPV IAAVNGYALG GGCELAMMCD
160 170 180 190 200
IIYAGEKAQF GQPEILLGTI PGAGGTQRLT RAVGKSLAME MVLTGDRISA
210 220 230 240 250
QDAKQAGLVS KIFPVETLVE EAIQCAEKIA NNSKIIVAMA KESVNAAFEM
260 270 280 290
TLTEGNKLEK KLFYSTFATD DRREGMSAFV EKRKANFKDH
Length:290
Mass (Da):31,516
Last modified:April 1, 1990 - v1
Checksum:i1E528590961D0CC0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15958 mRNA Translation: CAA34080.1
BC064655 mRNA Translation: AAH64655.1
PIRiS06477
RefSeqiNP_511178.1, NM_078623.2
XP_003748934.1, XM_003748886.3
UniGeneiRn.6847

Genome annotation databases

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

Similar proteinsi

Entry informationi

Entry nameiECHM_RAT
AccessioniPrimary (citable) accession number: P14604
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 23, 2018
This is version 156 of the entry and version 1 of the sequence. See 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

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