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Protein

Enoyl-CoA hydratase, mitochondrial

Gene

Echs1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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.By similarity

Catalytic activityi

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

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 sitei141 – 1411Substrate; via amide nitrogenBy similarity
Sitei164 – 1641Important for catalytic activityBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-MMU-77310. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
R-MMU-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-MMU-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
R-MMU-77350. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
R-MMU-77352. Beta oxidation of butanoyl-CoA to acetyl-CoA.
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2136460. Echs1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727MitochondrionBy similarityAdd
BLAST
Chaini28 – 290263Enoyl-CoA hydratase, mitochondrialPRO_0000007412Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011N6-acetyllysine; alternateCombined sources
Modified residuei101 – 1011N6-succinyllysine; alternateCombined sources
Modified residuei114 – 1141PhosphoserineBy similarity
Modified residuei115 – 1151N6-acetyllysine; alternateCombined sources
Modified residuei115 – 1151N6-succinyllysine; alternateCombined sources
Modified residuei204 – 2041N6-succinyllysineCombined sources
Modified residuei211 – 2111N6-acetyllysineCombined sources
Modified residuei217 – 2171N6-acetyllysine; alternateCombined sources
Modified residuei217 – 2171N6-succinyllysine; alternateCombined sources

Post-translational modificationi

Acetylation of Lys-101 is observed in liver mitochondria from fasted mice but not from fed mice.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8BH95.
MaxQBiQ8BH95.
PaxDbiQ8BH95.
PRIDEiQ8BH95.

2D gel databases

REPRODUCTION-2DPAGEQ8BH95.

PTM databases

iPTMnetiQ8BH95.
PhosphoSiteiQ8BH95.
SwissPalmiQ8BH95.

Expressioni

Gene expression databases

BgeeiQ8BH95.
ExpressionAtlasiQ8BH95. baseline and differential.
GenevisibleiQ8BH95. MM.

Interactioni

Subunit structurei

Homohexamer; dimer of trimers.By similarity

Protein-protein interaction databases

IntActiQ8BH95. 2 interactions.
MINTiMINT-1859826.
STRINGi10090.ENSMUSP00000026538.

Structurei

3D structure databases

ProteinModelPortaliQ8BH95.
SMRiQ8BH95. Positions 31-290.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1680. Eukaryota.
COG1024. LUCA.
GeneTreeiENSGT00760000119100.
HOGENOMiHOG000027939.
HOVERGENiHBG010157.
InParanoidiQ8BH95.
KOiK07511.
OMAiSKAMEMV.
OrthoDBiEOG7N63NC.
PhylomeDBiQ8BH95.
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.

Q8BH95-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALRALLPR ACSSLLSSVR CPELRRFASG ANFQYIITEK KGKNSSVGLI
60 70 80 90 100
QLNRPKALNA LCNGLIEELN QALETFEQDP AVGAIVLTGG DKAFAAGADI
110 120 130 140 150
KEMQNRTFQD CYSSKFLSHW DHITRVKKPV IAAVNGYALG GGCELAMMCD
160 170 180 190 200
IIYAGEKAQF GQPEILLGTI PGAGGTQRLT RAVGKSLAME MVLTGDRISA
210 220 230 240 250
QDAKQAGLVS KIFPVEKLVE EAIQCAEKIA SNSKIVVAMA KESVNAAFEM
260 270 280 290
TLTEGNKLEK RLFYSTFATD DRREGMTAFV EKRKANFKDH
Length:290
Mass (Da):31,474
Last modified:March 1, 2003 - v1
Checksum:i3E51E529CE756C68
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711Q → L in AAH02178 (PubMed:15489334).Curated
Sequence conflicti172 – 1721G → R in AAH72658 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK040391 mRNA. Translation: BAC30583.1.
AK044954 mRNA. Translation: BAC32157.1.
AK088018 mRNA. Translation: BAC40099.1.
AK167404 mRNA. Translation: BAE39493.1.
BC002178 mRNA. Translation: AAH02178.1.
BC057971 mRNA. Translation: AAH57971.1.
BC072658 mRNA. Translation: AAH72658.1.
CCDSiCCDS21964.1.
RefSeqiNP_444349.1. NM_053119.2.
UniGeneiMm.24452.
Mm.486735.

Genome annotation databases

EnsembliENSMUST00000026538; ENSMUSP00000026538; ENSMUSG00000025465.
GeneIDi93747.
KEGGimmu:93747.
UCSCiuc009kgx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK040391 mRNA. Translation: BAC30583.1.
AK044954 mRNA. Translation: BAC32157.1.
AK088018 mRNA. Translation: BAC40099.1.
AK167404 mRNA. Translation: BAE39493.1.
BC002178 mRNA. Translation: AAH02178.1.
BC057971 mRNA. Translation: AAH57971.1.
BC072658 mRNA. Translation: AAH72658.1.
CCDSiCCDS21964.1.
RefSeqiNP_444349.1. NM_053119.2.
UniGeneiMm.24452.
Mm.486735.

3D structure databases

ProteinModelPortaliQ8BH95.
SMRiQ8BH95. Positions 31-290.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BH95. 2 interactions.
MINTiMINT-1859826.
STRINGi10090.ENSMUSP00000026538.

PTM databases

iPTMnetiQ8BH95.
PhosphoSiteiQ8BH95.
SwissPalmiQ8BH95.

2D gel databases

REPRODUCTION-2DPAGEQ8BH95.

Proteomic databases

EPDiQ8BH95.
MaxQBiQ8BH95.
PaxDbiQ8BH95.
PRIDEiQ8BH95.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026538; ENSMUSP00000026538; ENSMUSG00000025465.
GeneIDi93747.
KEGGimmu:93747.
UCSCiuc009kgx.1. mouse.

Organism-specific databases

CTDi1892.
MGIiMGI:2136460. Echs1.

Phylogenomic databases

eggNOGiKOG1680. Eukaryota.
COG1024. LUCA.
GeneTreeiENSGT00760000119100.
HOGENOMiHOG000027939.
HOVERGENiHBG010157.
InParanoidiQ8BH95.
KOiK07511.
OMAiSKAMEMV.
OrthoDBiEOG7N63NC.
PhylomeDBiQ8BH95.
TreeFamiTF314497.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiEchs1. mouse.
NextBioi351613.
PROiQ8BH95.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BH95.
ExpressionAtlasiQ8BH95. baseline and differential.
GenevisibleiQ8BH95. MM.

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

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Liver and Thymus.
  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].
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain and Mammary gland.
  3. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 116-125; 158-178 AND 274-282, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain and Hippocampus.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-101; LYS-115; LYS-204 AND LYS-217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101; LYS-115; LYS-211 AND LYS-217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiECHM_MOUSE
AccessioniPrimary (citable) accession number: Q8BH95
Secondary accession number(s): Q3TJK2
, Q6GQS2, Q6PEN1, Q99LX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 1, 2003
Last modified: March 16, 2016
This is version 112 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.