UniProtKB - P14604 (ECHM_RAT)
Protein
Enoyl-CoA hydratase, mitochondrial
Gene
Echs1
Organism
Rattus norvegicus (Rat)
Status
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
- EC:4.2.1.17By similarityThis reaction proceeds in the backwardBy similarity direction.
- EC:4.2.1.17By similarityThis reaction proceeds in the backwardBy similarity direction.
- This reaction proceeds in the backward1 Publication direction.
- This reaction proceeds in the backwardBy similarity direction.
- This reaction proceeds in the backwardBy similarity direction.
- This reaction proceeds in the backwardBy similarity direction.
: fatty acid beta-oxidation Pathwayi
This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.By similarityView all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 141 | Substrate; via amide nitrogen | 1 | |
Sitei | 164 | Important for catalytic activity | 1 |
GO - Molecular functioni
- 3-hydroxypropionyl-CoA dehydratase activity Source: RHEA
- crotonyl-CoA hydratase activity Source: RHEA
- enoyl-CoA hydratase activity Source: RGD
GO - Biological processi
- fatty acid beta-oxidation Source: RGD
Keywordsi
Molecular function | Lyase |
Biological process | Fatty acid metabolism, Lipid metabolism |
Enzyme and pathway databases
BRENDAi | 4.2.1.17, 5301 |
Reactomei | R-RNO-70895, Branched-chain amino acid catabolism R-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 |
UniPathwayi | UPA00659 |
Chemistry databases
SwissLipidsi | SLP:000001128 |
Names & Taxonomyi
Protein namesi | Recommended name: Enoyl-CoA hydratase, mitochondrialCurated (EC:4.2.1.17By similarity)Alternative name(s): Enoyl-CoA hydratase 1 Short-chain enoyl-CoA hydratase Short name: SCEH |
Gene namesi | Name:Echs1Imported |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 69330, Echs1 |
Subcellular locationi
Mitochondrion
- Mitochondrion matrix 1 Publication
Mitochondrion
- mitochondrial matrix Source: UniProtKB-SubCell
- mitochondrion Source: RGD
Keywords - Cellular componenti
MitochondrionPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 144 | E → D: Reduces activity 50-fold. 1 Publication | 1 | |
Mutagenesisi | 144 | E → Q: Reduces activity 3300-fold. 1 Publication | 1 | |
Mutagenesisi | 164 | E → D: Reduces activity 1250-fold. 1 Publication | 1 | |
Mutagenesisi | 164 | E → Q: Reduces activity 330000-fold. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL3153 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 29 | Mitochondrion1 PublicationAdd BLAST | 29 | |
ChainiPRO_0000007414 | 30 – 290 | Enoyl-CoA hydratase, mitochondrialAdd BLAST | 261 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 101 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 101 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 115 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 115 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 204 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 211 | N6-acetyllysineBy similarity | 1 |
Keywords - PTMi
AcetylationProteomic databases
jPOSTi | P14604 |
PaxDbi | P14604 |
PRIDEi | P14604 |
PTM databases
iPTMneti | P14604 |
PhosphoSitePlusi | P14604 |
Expressioni
Tissue specificityi
Detected in liver (at protein level).1 Publication
Gene expression databases
Bgeei | ENSRNOG00000018522, Expressed in liver and 21 other tissues |
Genevisiblei | P14604, RN |
Interactioni
Subunit structurei
Homohexamer; dimer of trimers.
4 PublicationsProtein-protein interaction databases
BioGRIDi | 250789, 1 interactor |
IntActi | P14604, 9 interactors |
STRINGi | 10116.ENSRNOP00000066388 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P14604 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P14604 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 98 – 101 | Substrate binding | 4 |
Sequence similaritiesi
Belongs to the enoyl-CoA hydratase/isomerase family.Curated
Keywords - Domaini
Transit peptidePhylogenomic databases
eggNOGi | KOG1680, Eukaryota |
GeneTreei | ENSGT00940000157609 |
HOGENOMi | CLU_009834_7_6_1 |
InParanoidi | P14604 |
OMAi | IFKQTDA |
OrthoDBi | 1221604at2759 |
PhylomeDBi | P14604 |
TreeFami | TF314497 |
Family and domain databases
Gene3Di | 1.10.12.10, 1 hit |
InterProi | View 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 |
Pfami | View protein in Pfam PF00378, ECH_1, 1 hit |
SUPFAMi | SSF52096, SSF52096, 1 hit |
PROSITEi | View protein in PROSITE PS00166, ENOYL_COA_HYDRATASE, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P14604-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi 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_003748886.3 |
Genome annotation databases
Ensembli | ENSRNOT00000025446; ENSRNOP00000025446; ENSRNOG00000018522 ENSRNOT00000071574; ENSRNOP00000066388; ENSRNOG00000047565 |
GeneIDi | 100911186 140547 |
KEGGi | rno:100911186 rno:140547 |
UCSCi | RGD:69330, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi 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_003748886.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
SMRi | P14604 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 250789, 1 interactor |
IntActi | P14604, 9 interactors |
STRINGi | 10116.ENSRNOP00000066388 |
Chemistry databases
ChEMBLi | CHEMBL3153 |
SwissLipidsi | SLP:000001128 |
PTM databases
iPTMneti | P14604 |
PhosphoSitePlusi | P14604 |
Proteomic databases
jPOSTi | P14604 |
PaxDbi | P14604 |
PRIDEi | P14604 |
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 | KOG1680, Eukaryota |
GeneTreei | ENSGT00940000157609 |
HOGENOMi | CLU_009834_7_6_1 |
InParanoidi | P14604 |
OMAi | IFKQTDA |
OrthoDBi | 1221604at2759 |
PhylomeDBi | P14604 |
TreeFami | TF314497 |
Enzyme and pathway databases
UniPathwayi | UPA00659 |
BRENDAi | 4.2.1.17, 5301 |
Reactomei | R-RNO-70895, Branched-chain amino acid catabolism R-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 |
Miscellaneous databases
EvolutionaryTracei | P14604 |
PROi | PR:P14604 |
Gene expression databases
Bgeei | ENSRNOG00000018522, Expressed in liver and 21 other tissues |
Genevisiblei | P14604, RN |
Family and domain databases
Gene3Di | 1.10.12.10, 1 hit |
InterProi | View 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 |
Pfami | View protein in Pfam PF00378, ECH_1, 1 hit |
SUPFAMi | SSF52096, SSF52096, 1 hit |
PROSITEi | View protein in PROSITE PS00166, ENOYL_COA_HYDRATASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ECHM_RAT | |
Accessioni | P14604Primary (citable) accession number: P14604 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1990 |
Last sequence update: | April 1, 1990 | |
Last modified: | April 7, 2021 | |
This is version 174 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families