P30084 (ECHM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

ECHS1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	290 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate.
Catalytic activity	(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subunit structure	Homohexamer; dimer of trimers. Ref.11
Subcellular location	Mitochondrion matrix.
Tissue specificity	Liver, fibroblast, muscle. Barely detectable in spleen and kidney.
Sequence similarities	Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Molecular function	Lyase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid beta-oxidation Traceable author statement. Source: Reactome
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome
Molecular_function	enoyl-CoA hydratase activity Traceable author statement. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 27

27

Mitochondrion Ref.6

Chain

28 – 290

263

Enoyl-CoA hydratase, mitochondrial

PRO_0000007411

Regions

Region

98 – 101

4

Substrate binding

Sites

Binding site

141

1

Substrate; via amide nitrogen

Site

164

1

Important for catalytic activity By similarity

Amino acid modifications

Modified residue

101

1

N6-acetyllysine By similarity

Modified residue

118

1

N6-acetyllysine Ref.9

Natural variations

Natural variant

11

1

V → A. Ref.1 Ref.2
Corresponds to variant rs10466126 [ dbSNP | Ensembl ].

VAR_022273

Natural variant

75

1

T → I. Ref.1 Ref.2 Ref.3 Ref.5 Ref.8
Corresponds to variant rs1049951 [ dbSNP | Ensembl ].

VAR_022274

Experimental info

Sequence conflict

84

1

A → G in BAA03001. Ref.1

Sequence conflict

121

1

D → G in BAA03001. Ref.1

Sequence conflict

138

1

A → P in BAA03001. Ref.1

Sequence conflict

188 – 189

2

AM → EL in BAA03001. Ref.1

Sequence conflict

197

1

R → A in BAA03001. Ref.1

Secondary structure

1

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290

Helix Strand Turn

Details...

Beta strand

34 – 42

9

Helix

43 – 45

3

Beta strand

47 – 52

6

Helix

55 – 57

3

Helix

63 – 78

16

Beta strand

84 – 88

5

Beta strand

91 – 95

5

Helix

100 – 103

4

Helix

108 – 113

6

Turn

114 – 117

4

Helix

119 – 125

7

Beta strand

130 – 134

5

Beta strand

136 – 139

4

Helix

141 – 147

7

Beta strand

149 – 155

7

Beta strand

159 – 161

3

Helix

163 – 167

5

Beta strand

172 – 174

3

Turn

175 – 177

3

Helix

178 – 183

6

Helix

185 – 194

10

Helix

200 – 205

6

Beta strand

210 – 213

4

Turn

215 – 217

3

Helix

218 – 231

14

Helix

234 – 245

12

Helix

246 – 248

3

Helix

252 – 266

15

Helix

270 – 280

11

Sequences

	Sequence		Length	Mass (Da)
	P30084 [UniParc]. Last modified April 26, 2005. Version 4. Checksum: 0CCD0C7F891B1704	FASTA	290	31,387
	10 20 30 40 50 60 MAALRVLLSC VRGPLRPPVR CPAWRPFASG ANFEYIIAEK RGKNNTVGLI QLNRPKALNA 70 80 90 100 110 120 LCDGLIDELN QALKTFEEDP AVGAIVLTGG DKAFAAGADI KEMQNLSFQD CYSSKFLKHW 130 140 150 160 170 180 DHLTQVKKPV IAAVNGYAFG GGCELAMMCD IIYAGEKAQF AQPEILIGTI PGAGGTQRLT 190 200 210 220 230 240 RAVGKSLAME MVLTGDRISA QDAKQAGLVS KICPVETLVE EAIQCAEKIA SNSKIVVAMA 250 260 270 280 290 KESVNAAFEM TLTEGSKLEK KLFYSTFATD DRKEGMTAFV EKRKANFKDQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequence analysis of the cDNA for human mitochondrial short-chain enoyl-CoA hydratase." Kanazawa M., Ohtake A., Abe H., Yamamoto S., Satoh Y., Takayanagi M., Niimi H., Mori M., Hashimoto T. Enzyme Protein 47:9-13(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-11 AND ILE-75. Tissue: Liver.
[2]	"Human mitochondrial enoyl-CoA hydratase gene (ECHS1): structural organization and assignment to chromosome 10q26.2-q26.3." Janssen U., Davis E.M., le Beau M.M., Stoffel W. Genomics 40:470-475(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-11 AND ILE-75.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-75.
[4]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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], VARIANT ILE-75. Tissue: Placenta.
[6]	"Human liver protein map: a reference database established by microsequencing and gel comparison." Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J. Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-37. Tissue: Liver.
[7]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 44-56; 102-115; 158-178; 186-197; 242-257 AND 262-273, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[8]	"Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping." Hubbard M.J., McHugh N.J. Electrophoresis 21:3785-3796(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 57-63; 75-92 AND 158-178, VARIANT ILE-75, MASS SPECTROMETRY. Tissue: Liver.
[9]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118, MASS SPECTROMETRY.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"The crystal structure of human enoyl-coenzyme A (CoA) hydratase short chain 1, ECHS1." Structural genomics consortium (SGC) Submitted (AUG-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 24-290 IN COMPLEX WITH CROTONYL COENZYME A, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00024993.

RefSeq

NP_004083.3. NM_004092.3.

UniGene

Hs.76394.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HW5	X-ray	2.55	A/B/C/D/E/F	28-290	[»]

ProteinModelPortal

P30084.

ModBase

Search...

Protein-protein interaction databases

IntAct

P30084. 11 interactions.

MINT

MINT-1401929.

STRING

9606.ENSP00000357535.

PTM databases

PhosphoSite

P30084.

Polymorphism databases

DMDM

62906863.

2D gel databases

DOSAC-COBS-2DPAGE

P30084.

REPRODUCTION-2DPAGE

IPI00024993.
P30084.

SWISS-2DPAGE

P30084.

UCD-2DPAGE

P30084.

Proteomic databases

PaxDb

P30084.

PeptideAtlas

P30084.

PRIDE

P30084.

Protocols and materials databases

DNASU

1892.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368547; ENSP00000357535; ENSG00000127884.

GeneID

1892.

KEGG

hsa:1892.

UCSC

uc001lmu.3. human.

Organism-specific databases

CTD

1892.

GeneCards

GC10M135175.

HGNC

HGNC:3151. ECHS1.

HPA

CAB003783.
HPA021995.
HPA022476.

MIM

602292. gene.

neXtProt

NX_P30084.

PharmGKB

PA27597.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1024.

HOGENOM

HOG000027939.

HOVERGEN

HBG010157.

InParanoid

P30084.

KO

K07511.

OMA

NFEYIIA.

OrthoDB

EOG4P2Q32.

PhylomeDB

P30084.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

UniPathway

UPA00659.

Gene expression databases

Bgee

P30084.

CleanEx

HS_ECHS1.

Genevestigator

P30084.

GermOnline

ENSG00000127884. Homo sapiens.

Family and domain databases

InterPro

IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]

Pfam

PF00378. ECH. 1 hit.
[Graphical view]

PROSITE

PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ECHS1. human.

EvolutionaryTrace

P30084.

GenomeRNAi

1892.

NextBio

7715.

SOURCE

Search...

Entry information

Entry name

ECHM_HUMAN

Accession

Primary (citable) accession number: P30084
Secondary accession number(s): O00739, Q5VWY1, Q96H54

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 26, 2005
Last modified:	May 1, 2013
This is version 142 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.