Reviewed, UniProtKB/Swiss-Prot P30084 (ECHM_HUMAN)

Names and origin

Protein names

Recommended name:
    Enoyl-CoA hydratase, mitochondrial
    EC=4.2.1.17
Alternative name(s):
    Short chain enoyl-CoA hydratase
      Short name=SCEH
    Enoyl-CoA hydratase 1

Gene names

Name:

ECHS1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.10
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
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Ref.2 Traceable author statement. Source: ProtInc
Cellular component	mitochondrial matrix Inferred from Experiment. Source: Reactome
Molecular function	enoyl-CoA hydratase activity Ref.2 Inferred from Experiment. Source: Reactome protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EPB41	P11171	1	EBI-719602,EBI-1050906

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

Natural variations

Natural variant

11

1

V → A: dbSNP rs10466126. Ref.1 Ref.2

VAR_022273

Natural variant

75

1

T → I: dbSNP rs1049951. Ref.1 Ref.2 Ref.3 Ref.5 Ref.8

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)
	P30084-1 [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: 8012501] [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: 9073515] [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: 15164054] [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: 15489334] [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: 1286669] [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: 11271497] [Abstract] Cited for: PROTEIN SEQUENCE OF 57-63; 75-92 AND 158-178, VARIANT ILE-75, MASS SPECTROMETRY. Tissue: Liver.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]	"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

EMBLGenBankDDBJ

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.

UniGene

Hs.76394

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

IntAct

P30084. 19 interactions.

PTM databases

PhosphoSite

P30084.

2-D gel databases

SWISS-2DPAGE

P30084.

DOSAC-COBS-2DPAGE

P30084.

REPRODUCTION-2DPAGE

IPI00024993.
P30084.

Siena-2DPAGE

P30084.

Proteomic databases

PeptideAtlas

P30084.

PRIDE

P30084.

Genome annotation databases

Ensembl

ENSG00000127884. Homo sapiens. [Contig view]

GeneID

1892.

KEGG

hsa:1892.

NMPDR

fig|9606.3.peg.4902.

UCSC

uc001lmu.1. human.

Organism-specific databases

GeneCards

GC10M135025.

H-InvDB

HIX0009333.

HGNC

HGNC:3151. ECHS1.

HPA

CAB003783.

MIM

602292. gene.

PharmGKB

PA27597.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P30084.

HOVERGEN

P30084.

OMA

P30084. IKEMQNL.

Enzyme and pathway databases

BRENDA

4.2.1.17. 247.

Reactome

REACT_13. Metabolism of amino acids.
REACT_602. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

P30084.

Bgee

P30084.

CleanEx

HS_ECHS1.

GermOnline

ENSG00000127884. Homo sapiens.

Family and domain databases

InterPro

IPR001753. Crotonase_core.
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 Resources

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:	July 7, 2009
This is version 104 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)