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Q58DM8 (ECHM_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length290 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate By similarity.

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 By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionLyase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processfatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionenoyl-CoA hydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion By similarity
Chain28 – 290263Enoyl-CoA hydratase, mitochondrial
PRO_0000007410

Regions

Region98 – 1014Substrate binding By similarity

Sites

Binding site1411Substrate; via amide nitrogen By similarity
Site1641Important for catalytic activity By similarity

Amino acid modifications

Modified residue1011N6-acetyllysine By similarity

Experimental info

Sequence conflict1981I → N in AAI09606. Ref.3
Sequence conflict269 – 2779TEDRKEGMA → PKTGRKAWP in AAY83884. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q58DM8 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 30CAD9F7314AD50F

FASTA29031,243
        10         20         30         40         50         60 
MAALRALLPR VRAPLRPWLF CPVQRSFASS AAFEYIITAK KGRNSNVGLI QLNRPKALNA 

        70         80         90        100        110        120 
LCNGLIVELN QALQAFEEDP AVGAIVLTGG EKVFAAGADI KEMQSLTFQN CYSGGFLSHW 

       130        140        150        160        170        180 
DQLTRVKKPV IAAVNGYALG GGCELAMMCD IIYAGEKAQF GQPEILIGTI PGAGGTQRLT 

       190        200        210        220        230        240 
RAVGKSLAME MVLTGDRISA QDAKQAGLVS KIFPVETVVE EAIQCAEKIA SNSKIVTAMA 

       250        260        270        280        290 
KESVNAAFEM TLAEGVKLEK KLFYSTFATE DRKEGMAAFV EKRKANFKDQ 

« Hide

References

« Hide 'large scale' references
[1]"Comparative mapping of the bovine SPRN locus."
Ferretti L., Uboldi C., Del Vecchio I., Eggen A., Brunner R., Iannuzzi L.
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ058610 mRNA. Translation: AAY83884.1.
DQ058603 Genomic DNA. Translation: AAY83878.1.
BT021569 mRNA. Translation: AAX46416.1.
BC109605 mRNA. Translation: AAI09606.1.
IPIIPI00701876.
RefSeqNP_001020377.2. NM_001025206.2.
UniGeneBt.64629.

3D structure databases

ProteinModelPortalQ58DM8.
SMRQ58DM8. Positions 31-290.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ58DM8.

Proteomic databases

PRIDEQ58DM8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000044947; ENSBTAP00000042386; ENSBTAG00000017710.
GeneID281748.
KEGGbta:281748.

Organism-specific databases

CTD1892.

Phylogenomic databases

eggNOGmaNOG05271.
GeneTreeENSGT00580000081296.
HOVERGENHBG010157.
InParanoidQ58DM8.
OMATGNMINA.
OrthoDBEOG4P2Q32.
PhylomeDBQ58DM8.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11697.

Family and domain databases

InterProIPR014748. Crontonase_C.
IPR001753. Crotonase_core.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
Gene3DG3DSA:1.10.12.10. Crontonase_C. 1 hit.
KOK07511.
PfamPF00378. ECH. 1 hit.
[Graphical view]
PROSITEPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameECHM_BOVIN
AccessionPrimary (citable) accession number: Q58DM8
Secondary accession number(s): Q2TBV2, Q4PS76
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: April 26, 2005
Last modified: November 16, 2011
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families