[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 30-39 AND 80-94. TISSUE=Liver; PubMed=2806264 [NCBI, ExPASy, EBI, Israel, Japan] Minami-Ishii N., Taketani S., Osumi T., Hashimoto T.; "Molecular cloning and sequence analysis of the cDNA for rat mitochondrial enoyl-CoA hydratase. Structural and evolutionary relationships linked to the bifunctional enzyme of the peroxisomal beta-oxidation system."; Eur. J. Biochem. 185:73-78(1989).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Prostate; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). TISSUE=Liver; PubMed=8895557 [NCBI, ExPASy, EBI, Israel, Japan] Engel C.K., Mathieu M., Zeelen J.P., Hiltunen J.K., Wierenga R.K.; "Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5-A resolution: a spiral fold defines the CoA-binding pocket."; EMBO J. 15:5135-5145(1996).
[4]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). TISSUE=Liver; DOI=10.1006/jmbi.1997.1491; PubMed=9480773 [NCBI, ExPASy, EBI, Israel, Japan] Engel C.K., Kiema T.R., Hiltunen J.K., Wierenga R.K.; "The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule."; J. Mol. Biol. 275:847-859(1998).

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: Homohexamer; dimer of trimers.
SUBCELLULAR LOCATION: Mitochondrion matrix.
DOMAIN: The monomer is folded into a right-handed spiral of four turns, followed by two small domains which are involved in trimerization.
SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X15958; CAA34080.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC064655; AAH64655.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S06477; S06477.

NP_511178.1; -.

3D structure databases

PDB

1DUB; X-ray; 2.50 A; A/B/C/D/E/F=30-290.	[ExPASy / RCSB / EBI]
1EY3; X-ray; 2.30 A; A/B/C/D/E/F=33-290.	[ExPASy / RCSB / EBI]
1MJ3; X-ray; 2.10 A; A/B/C/D/E/F=31-290.	[ExPASy / RCSB / EBI]
2DUB; X-ray; 2.40 A; A/B/C/D/E/F=30-290.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DUB; -.
1EY3; -.
1MJ3; -.
2DUB; -.

ModBase

P14604.

Protein-protein interaction databases

IntAct

P14604; -.

2D gel databases

Rat-heart-2DPAGE

P14604; -.

Organism-specific databases

RGD

69330; Echs1.

Gene expression databases

ArrayExpress

P14604; -.

GermOnline

ENSRNOG00000018522; Rattus norvegicus.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.

Family and domain databases

InterPro

IPR001753; Crotonase_core.
Graphical view of domain structure.

Pfam

PF00378; ECH; 1.
Pfam graphical view of domain structure.

PROSITE

PS00166; ENOYL_COA_HYDRATASE; 1.

BLOCKS

P14604.

Genome annotation databases

Ensembl

ENSRNOG00000018522; Rattus norvegicus. [Contig view]

GeneID

140547; -.

KEGG

rno:140547; -.

NMPDR

fig|10116.3.peg.3204; -.

Phylogenomic databases

HOVERGEN

P14604; -.

Other

P14604; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Direct protein sequencing; Fatty acid metabolism; Lipid metabolism; Lyase; Mitochondrion; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 29`	`29`	`Mitochondrion.`
`CHAIN`	`30 290`	`261`	`Enoyl-CoA hydratase, mitochondrial.`	`PRO_0000007414`
`ACT_SITE`	`144 144`		`Proton acceptor.`
`ACT_SITE`	`164 164`		`Proton donor.`
`MOD_RES`	`101 101`		`N6-acetyllysine (By similarity).`
`STRAND`	`35 40`	`6`
`STRAND`	`42 45`	`4`
`STRAND`	`47 52`	`6`
`HELIX`	`55 57`	`3`
`HELIX`	`63 78`	`16`
`STRAND`	`84 88`	`5`
`STRAND`	`91 95`	`5`
`HELIX`	`100 103`	`4`
`HELIX`	`108 111`	`4`
`HELIX`	`122 125`	`4`
`STRAND`	`130 134`	`5`
`STRAND`	`136 139`	`4`
`HELIX`	`141 148`	`8`
`STRAND`	`149 155`	`7`
`STRAND`	`159 161`	`3`
`HELIX`	`163 167`	`5`
`TURN`	`175 177`	`3`
`HELIX`	`178 183`	`6`
`HELIX`	`185 194`	`10`
`HELIX`	`200 205`	`6`
`STRAND`	`210 213`	`4`
`TURN`	`215 217`	`3`
`HELIX`	`218 230`	`13`
`HELIX`	`234 245`	`12`
`HELIX`	`246 248`	`3`
`HELIX`	`252 265`	`14`
`HELIX`	`266 268`	`3`
`HELIX`	`270 280`	`11`

Sequence information

Length: 290 AA [This is the length of the unprocessed precursor]

Molecular weight: 31516 Da [This is the MW of the unprocessed precursor]

CRC64: 1E528590961D0CC0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAALRALLPR ACNSLLSPVR CPEFRRFASG ANFQYIITEK KGKNSSVGLI QLNRPKALNA 

        70         80         90        100        110        120 
LCNGLIEELN QALETFEEDP AVGAIVLTGG EKAFAAGADI KEMQNRTFQD CYSGKFLSHW 

       130        140        150        160        170        180 
DHITRIKKPV IAAVNGYALG GGCELAMMCD IIYAGEKAQF GQPEILLGTI PGAGGTQRLT 

       190        200        210        220        230        240 
RAVGKSLAME MVLTGDRISA QDAKQAGLVS KIFPVETLVE EAIQCAEKIA NNSKIIVAMA 

       250        260        270        280        290 
KESVNAAFEM TLTEGNKLEK KLFYSTFATD DRREGMSAFV EKRKANFKDH

P14604 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools