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Protein

Enoyl-CoA hydratase, mitochondrial

Gene

ECHS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. 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.1 Publication

Catalytic activityi

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.1 Publication

Kineticsi

  1. KM=12.75 µM for crotonyl-CoA1 Publication
  2. KM=34.04 µM for acryloyl-CoA1 Publication
  3. KM=45.83 µM for 3-Methylcrotonyl-CoA1 Publication
  4. KM=57.87 µM for tiglyl-CoA1 Publication
  1. Vmax=54.64 µmol/min/mg enzyme toward crotonyl-CoA1 Publication
  2. Vmax=42.92 µmol/min/mg enzyme toward acryloyl-CoA1 Publication
  3. Vmax=49.02 µmol/min/mg enzyme toward 3-Methylcrotonyl-CoA1 Publication
  4. Vmax=6.66 µmol/min/mg enzyme toward tiglyl-CoA1 Publication

Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.1 Publication
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 activityBy similarity1

GO - Molecular functioni

  • enoyl-CoA hydratase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS05132-MONOMER.
ZFISH:HS05132-MONOMER.
BRENDAi4.2.1.17. 2681.
ReactomeiR-HSA-77310. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
R-HSA-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-HSA-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
R-HSA-77350. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
R-HSA-77352. Beta oxidation of butanoyl-CoA to acetyl-CoA.
SABIO-RKP30084.
UniPathwayiUPA00659.

Chemistry databases

SwissLipidsiSLP:000001471.

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-CoA hydratase, mitochondrial (EC:4.2.1.171 Publication)
Alternative name(s):
Enoyl-CoA hydratase 1
Short-chain enoyl-CoA hydratase
Short name:
SCEH
Gene namesi
Name:ECHS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:3151. ECHS1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Mitochondrial short-chain enoyl-CoA hydratase 1 deficiency (ECHS1D)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe, autosomal recessive inborn error affecting valine metabolism. Disease features include brain lesions in the basal ganglia, neurodegeneration, delayed psychomotor development, hypotonia, spasticity, and increased lactic acid in serum and cerebral serum fluid.
See also OMIM:616277
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0733732A → V in ECHS1D. 1 PublicationCorresponds to variant rs587776498dbSNPEnsembl.1
Natural variantiVAR_07618533F → S in ECHS1D. 2 Publications1
Natural variantiVAR_07618654R → H in ECHS1D. 1 PublicationCorresponds to variant rs375266808dbSNPEnsembl.1
Natural variantiVAR_07618759N → S in ECHS1D; decreases significantly enoyl-CoA hydratase activity; decreases significantly protein expression. 3 PublicationsCorresponds to variant rs201865375dbSNPEnsembl.1
Natural variantiVAR_07618866I → T in ECHS1D. 1 PublicationCorresponds to variant rs371063211dbSNPEnsembl.1
Natural variantiVAR_07618977E → Q in ECHS1D. 1 Publication1
Natural variantiVAR_07619090G → R in ECHS1D; unknown pathological significance. 1 Publication1
Natural variantiVAR_076191132A → T in ECHS1D. 1 PublicationCorresponds to variant rs770931871dbSNPEnsembl.1
Natural variantiVAR_076479138A → V in ECHS1D; decreases enoyl-CoA hydratase activity of 70%; decreases significantly protein expression. 1 Publication1
Natural variantiVAR_076192150D → G in ECHS1D. 1 Publication1
Natural variantiVAR_073374158A → D in ECHS1D. 1 PublicationCorresponds to variant rs786204001dbSNPEnsembl.1
Natural variantiVAR_076193159Q → R in ECHS1D. 2 PublicationsCorresponds to variant rs375032130dbSNPEnsembl.1
Natural variantiVAR_076194195G → S in ECHS1D. 1 PublicationCorresponds to variant rs761989177dbSNPEnsembl.1
Natural variantiVAR_076195225C → R in ECHS1D. 1 PublicationCorresponds to variant rs769429279dbSNPEnsembl.1
Natural variantiVAR_076196273K → E in ECHS1D. 1 PublicationCorresponds to variant rs565090080dbSNPEnsembl.1
Natural variantiVAR_076480281E → G in ECHS1D; unknown pathological significance. 1 Publication1

Keywords - Diseasei

Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNETi1892.
MIMi616277. phenotype.
OpenTargetsiENSG00000127884.
PharmGKBiPA27597.

Polymorphism and mutation databases

BioMutaiECHS1.
DMDMi62906863.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 27MitochondrionCombined sources1 PublicationAdd BLAST27
ChainiPRO_000000741128 – 290Enoyl-CoA hydratase, mitochondrialAdd BLAST263

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei46PhosphothreonineCombined sources1
Modified residuei101N6-acetyllysine; alternateBy similarity1
Modified residuei101N6-succinyllysine; alternateBy similarity1
Modified residuei114PhosphoserineCombined sources1
Modified residuei115N6-acetyllysine; alternateBy similarity1
Modified residuei115N6-succinyllysine; alternateBy similarity1
Modified residuei118N6-acetyllysineCombined sources1
Modified residuei204N6-succinyllysineBy similarity1
Modified residuei211N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP30084.
MaxQBiP30084.
PaxDbiP30084.
PeptideAtlasiP30084.
PRIDEiP30084.
TopDownProteomicsiP30084.

2D gel databases

DOSAC-COBS-2DPAGEP30084.
REPRODUCTION-2DPAGEIPI00024993.
P30084.
SWISS-2DPAGEP30084.
UCD-2DPAGEP30084.

PTM databases

iPTMnetiP30084.
PhosphoSitePlusiP30084.
SwissPalmiP30084.

Expressioni

Tissue specificityi

Liver, fibroblast, muscle. Barely detectable in spleen and kidney.

Gene expression databases

BgeeiENSG00000127884.
CleanExiHS_ECHS1.
GenevisibleiP30084. HS.

Organism-specific databases

HPAiCAB003783.
HPA021995.
HPA022476.

Interactioni

Subunit structurei

Homohexamer; dimer of trimers.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0072EBI-719602,EBI-5323863
STAT3P407633EBI-719602,EBI-518675
Stat3P422273EBI-719602,EBI-602878From a different organism.

Protein-protein interaction databases

BioGridi108221. 60 interactors.
IntActiP30084. 26 interactors.
MINTiMINT-1401929.
STRINGi9606.ENSP00000357535.

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
Turni114 – 117Combined sources4
Helixi119 – 125Combined sources7
Beta strandi130 – 134Combined sources5
Beta strandi136 – 139Combined sources4
Helixi141 – 147Combined sources7
Beta strandi149 – 155Combined sources7
Beta strandi159 – 161Combined sources3
Helixi163 – 167Combined sources5
Beta strandi172 – 174Combined sources3
Turni175 – 177Combined sources3
Helixi178 – 183Combined sources6
Helixi185 – 194Combined sources10
Helixi200 – 205Combined sources6
Beta strandi210 – 213Combined sources4
Turni215 – 217Combined sources3
Helixi218 – 231Combined sources14
Helixi234 – 245Combined sources12
Helixi246 – 248Combined sources3
Helixi252 – 266Combined sources15
Helixi270 – 280Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HW5X-ray2.55A/B/C/D/E/F28-290[»]
ProteinModelPortaliP30084.
SMRiP30084.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30084.

Family & Domainsi

Region

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

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1680. Eukaryota.
COG1024. LUCA.
GeneTreeiENSGT00760000119100.
HOGENOMiHOG000027939.
HOVERGENiHBG010157.
InParanoidiP30084.
KOiK07511.
OMAiVSKIYPV.
OrthoDBiEOG091G0MVQ.
PhylomeDBiP30084.
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. 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.

P30084-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALRVLLSC VRGPLRPPVR CPAWRPFASG ANFEYIIAEK RGKNNTVGLI
60 70 80 90 100
QLNRPKALNA LCDGLIDELN QALKTFEEDP AVGAIVLTGG DKAFAAGADI
110 120 130 140 150
KEMQNLSFQD CYSSKFLKHW DHLTQVKKPV IAAVNGYAFG GGCELAMMCD
160 170 180 190 200
IIYAGEKAQF AQPEILIGTI PGAGGTQRLT RAVGKSLAME MVLTGDRISA
210 220 230 240 250
QDAKQAGLVS KICPVETLVE EAIQCAEKIA SNSKIVVAMA KESVNAAFEM
260 270 280 290
TLTEGSKLEK KLFYSTFATD DRKEGMTAFV EKRKANFKDQ
Length:290
Mass (Da):31,387
Last modified:April 26, 2005 - v4
Checksum:i0CCD0C7F891B1704
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti84A → G in BAA03001 (PubMed:8012501).Curated1
Sequence conflicti121D → G in BAA03001 (PubMed:8012501).Curated1
Sequence conflicti138A → P in BAA03001 (PubMed:8012501).Curated1
Sequence conflicti188 – 189AM → EL in BAA03001 (PubMed:8012501).Curated2
Sequence conflicti197R → A in BAA03001 (PubMed:8012501).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0733732A → V in ECHS1D. 1 PublicationCorresponds to variant rs587776498dbSNPEnsembl.1
Natural variantiVAR_02227311V → A.2 PublicationsCorresponds to variant rs10466126dbSNPEnsembl.1
Natural variantiVAR_07618533F → S in ECHS1D. 2 Publications1
Natural variantiVAR_07618654R → H in ECHS1D. 1 PublicationCorresponds to variant rs375266808dbSNPEnsembl.1
Natural variantiVAR_07618759N → S in ECHS1D; decreases significantly enoyl-CoA hydratase activity; decreases significantly protein expression. 3 PublicationsCorresponds to variant rs201865375dbSNPEnsembl.1
Natural variantiVAR_07618866I → T in ECHS1D. 1 PublicationCorresponds to variant rs371063211dbSNPEnsembl.1
Natural variantiVAR_02227475T → I.5 PublicationsCorresponds to variant rs1049951dbSNPEnsembl.1
Natural variantiVAR_07618977E → Q in ECHS1D. 1 Publication1
Natural variantiVAR_07619090G → R in ECHS1D; unknown pathological significance. 1 Publication1
Natural variantiVAR_076191132A → T in ECHS1D. 1 PublicationCorresponds to variant rs770931871dbSNPEnsembl.1
Natural variantiVAR_076479138A → V in ECHS1D; decreases enoyl-CoA hydratase activity of 70%; decreases significantly protein expression. 1 Publication1
Natural variantiVAR_076192150D → G in ECHS1D. 1 Publication1
Natural variantiVAR_073374158A → D in ECHS1D. 1 PublicationCorresponds to variant rs786204001dbSNPEnsembl.1
Natural variantiVAR_076193159Q → R in ECHS1D. 2 PublicationsCorresponds to variant rs375032130dbSNPEnsembl.1
Natural variantiVAR_076194195G → S in ECHS1D. 1 PublicationCorresponds to variant rs761989177dbSNPEnsembl.1
Natural variantiVAR_076195225C → R in ECHS1D. 1 PublicationCorresponds to variant rs769429279dbSNPEnsembl.1
Natural variantiVAR_076196273K → E in ECHS1D. 1 PublicationCorresponds to variant rs565090080dbSNPEnsembl.1
Natural variantiVAR_076480281E → G in ECHS1D; unknown pathological significance. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13900 mRNA. Translation: BAA03001.1.
X98126
, X98127, X98128, X98129 Genomic DNA. Translation: CAA66808.1.
BT007123 mRNA. Translation: AAP35787.1.
AL360181 Genomic DNA. Translation: CAH70286.1.
BC008906 mRNA. Translation: AAH08906.1.
CCDSiCCDS7681.1.
RefSeqiNP_004083.3. NM_004092.3.
UniGeneiHs.76394.

Genome annotation databases

EnsembliENST00000368547; ENSP00000357535; ENSG00000127884.
GeneIDi1892.
KEGGihsa:1892.
UCSCiuc001lmu.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13900 mRNA. Translation: BAA03001.1.
X98126
, X98127, X98128, X98129 Genomic DNA. Translation: CAA66808.1.
BT007123 mRNA. Translation: AAP35787.1.
AL360181 Genomic DNA. Translation: CAH70286.1.
BC008906 mRNA. Translation: AAH08906.1.
CCDSiCCDS7681.1.
RefSeqiNP_004083.3. NM_004092.3.
UniGeneiHs.76394.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HW5X-ray2.55A/B/C/D/E/F28-290[»]
ProteinModelPortaliP30084.
SMRiP30084.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108221. 60 interactors.
IntActiP30084. 26 interactors.
MINTiMINT-1401929.
STRINGi9606.ENSP00000357535.

Chemistry databases

SwissLipidsiSLP:000001471.

PTM databases

iPTMnetiP30084.
PhosphoSitePlusiP30084.
SwissPalmiP30084.

Polymorphism and mutation databases

BioMutaiECHS1.
DMDMi62906863.

2D gel databases

DOSAC-COBS-2DPAGEP30084.
REPRODUCTION-2DPAGEIPI00024993.
P30084.
SWISS-2DPAGEP30084.
UCD-2DPAGEP30084.

Proteomic databases

EPDiP30084.
MaxQBiP30084.
PaxDbiP30084.
PeptideAtlasiP30084.
PRIDEiP30084.
TopDownProteomicsiP30084.

Protocols and materials databases

DNASUi1892.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368547; ENSP00000357535; ENSG00000127884.
GeneIDi1892.
KEGGihsa:1892.
UCSCiuc001lmu.4. human.

Organism-specific databases

CTDi1892.
DisGeNETi1892.
GeneCardsiECHS1.
HGNCiHGNC:3151. ECHS1.
HPAiCAB003783.
HPA021995.
HPA022476.
MIMi602292. gene.
616277. phenotype.
neXtProtiNX_P30084.
OpenTargetsiENSG00000127884.
PharmGKBiPA27597.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1680. Eukaryota.
COG1024. LUCA.
GeneTreeiENSGT00760000119100.
HOGENOMiHOG000027939.
HOVERGENiHBG010157.
InParanoidiP30084.
KOiK07511.
OMAiVSKIYPV.
OrthoDBiEOG091G0MVQ.
PhylomeDBiP30084.
TreeFamiTF314497.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciMetaCyc:HS05132-MONOMER.
ZFISH:HS05132-MONOMER.
BRENDAi4.2.1.17. 2681.
ReactomeiR-HSA-77310. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
R-HSA-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-HSA-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
R-HSA-77350. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
R-HSA-77352. Beta oxidation of butanoyl-CoA to acetyl-CoA.
SABIO-RKP30084.

Miscellaneous databases

ChiTaRSiECHS1. human.
EvolutionaryTraceiP30084.
GeneWikiiECHS1.
GenomeRNAii1892.
PROiP30084.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000127884.
CleanExiHS_ECHS1.
GenevisibleiP30084. HS.

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 nameiECHM_HUMAN
AccessioniPrimary (citable) accession number: P30084
Secondary accession number(s): O00739, Q5VWY1, Q96H54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 26, 2005
Last modified: November 30, 2016
This is version 180 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.