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Q6AYG5 (ECHD1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Ethylmalonyl-CoA decarboxylase

EC=4.1.1.94
Alternative name(s):
Enoyl-CoA hydratase domain-containing protein 1
Methylmalonyl-CoA decarboxylase
Short name=MMCD
EC=4.1.1.41
Gene names
Name:Echdc1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Decarboxylases ethylmalonyl-CoA decarboxylase, a potentially toxic metabolite, to form butyryl-CoA, suggesting it might be involved in metabolite proofreading. Also has methylmalonyl-CoA decarboxylase activity at lower level By similarity.

Catalytic activity

(S)-ethylmalonyl-CoA = butanoyl-CoA + CO2.

(S)-methylmalonyl-CoA = propanoyl-CoA + CO2.

Subcellular location

Cytoplasmcytosol By similarity.

Sequence similarities

Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionLyase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncarboxy-lyase activity

Inferred from sequence or structural similarity. Source: UniProtKB

methylmalonyl-CoA decarboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 299299Ethylmalonyl-CoA decarboxylase
PRO_0000273249

Amino acid modifications

Modified residue2091N6-acetyllysine; alternate By similarity
Modified residue2091N6-succinyllysine; alternate By similarity
Modified residue2931N6-succinyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6AYG5 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: B74CCD89B663C42E

FASTA29932,631
        10         20         30         40         50         60 
MAKSLLASSL SVRTKILQTG VSLYNTTHGF HEEEVKKILE QFPGGSIDLQ KKQNGIGILT 

        70         80         90        100        110        120 
LNNSNKMNAF SGAMMLQLLE RVIELENWTE GKGLIVHGAK NTFCSGSDLN AVKALSTPEN 

       130        140        150        160        170        180 
GVALSMFMQN TLTRFMRLPL ISVALVQGWA MGGGAELTTA CDFRLMTEES VIRFVHKEMG 

       190        200        210        220        230        240 
IVPSWGGASR LVEIIGSRQA LKVLSGTFKL DSKEALRIGL ADEVLQPSDE ATALEQAQEW 

       250        260        270        280        290 
LEQFVSGPAQ VIRGLKKSVC SGRELYLEEA LQNERDVLET LWGGPANLEA IAKKGKHTK 

« Hide

References

« Hide 'large scale' references
[1]"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].
Tissue: Testis.
[2]Lubec G., Afjehi-Sadat L.
Submitted (DEC-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 38-51, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
[3]"Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite proofreading."
Linster C.L., Noel G., Stroobant V., Vertommen D., Vincent M.F., Bommer G.T., Veiga-da-Cunha M., Van Schaftingen E.
J. Biol. Chem. 286:42992-43003(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC079052 mRNA. Translation: AAH79052.1.
RefSeqNP_001007735.1. NM_001007734.1.
XP_006227809.1. XM_006227747.1.
UniGeneRn.4220.

3D structure databases

ProteinModelPortalQ6AYG5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000015440.

Proteomic databases

PaxDbQ6AYG5.
PRIDEQ6AYG5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000015440; ENSRNOP00000015440; ENSRNOG00000011622.
GeneID361465.
KEGGrno:361465.
UCSCRGD:1359654. rat.

Organism-specific databases

CTD55862.
RGD1359654. Echdc1.

Phylogenomic databases

eggNOGCOG1024.
GeneTreeENSGT00720000108837.
HOGENOMHOG000007808.
HOVERGENHBG054783.
InParanoidQ6AYG5.
OMAHKHMGLV.
OrthoDBEOG79W95T.
PhylomeDBQ6AYG5.
TreeFamTF315986.

Gene expression databases

GenevestigatorQ6AYG5.

Family and domain databases

Gene3D3.90.226.10. 1 hit.
InterProIPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamPF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF52096. SSF52096. 1 hit.
PROSITEPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio676398.

Entry information

Entry nameECHD1_RAT
AccessionPrimary (citable) accession number: Q6AYG5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: September 13, 2004
Last modified: June 11, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families