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Q28C91 (ECHD1_XENTR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. 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
ORF Names:TGas092k23.1
OrganismXenopus tropicalis (Western clawed frog) (Silurana tropicalis) [Reference proteome]
Taxonomic identifier8364 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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
   Technical termComplete proteome
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_0000416274

Sequences

Sequence LengthMass (Da)Tools
Q28C91 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: A0452C4A22C4DDF0

FASTA29932,907
        10         20         30         40         50         60 
MGIFVCRNSL RMLNVRWLYH RCLSLYNSNH GFNEAKIKEK LAQFTGGSVD LSKMDNGIAE 

        70         80         90        100        110        120 
ICINNPSRMN AFTGTMMIEL EERISDLENW KNGKGLIVYG AENTFCSGSD LNAVKAISNP 

       130        140        150        160        170        180 
QEGMMMCMLM QNTLTRLQRL PLISVALIQG KALGGGAELC TACDFRLMTE GSEIRFVHKQ 

       190        200        210        220        230        240 
MGLVPGWGGA ARLIHLIGSR HALKLLSGAL RVHPENALEL GLADNILLGT EDGFLSEAEN 

       250        260        270        280        290 
WIMPYIKGPS DVSRAVKKVI ISGREQKLED ALRTEKEIFG TVWGGLANLQ ALAKGTKHK 

« Hide

References

[1]Sanger Xenopus tropicalis EST/cDNA project
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Gastrula.
[2]"The genome of the Western clawed frog Xenopus tropicalis."
Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R., Gerhard D.S. expand/collapse author list , Goodstein D., Graves T., Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M., Rokhsar D.S.
Science 328:633-636(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]NIH - Xenopus Gene Collection (XGC) project
Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: N6.
Tissue: Gastrula and Ovary.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR942395 mRNA. Translation: CAJ83594.1.
AAMC01103784 Genomic DNA. No translation available.
BC088780 mRNA. Translation: AAH88780.1.
BC118874 mRNA. Translation: AAI18875.1.
BC170562 mRNA. Translation: AAI70562.1.
BC170919 mRNA. Translation: AAI70919.1.
RefSeqNP_001037862.1. NM_001044397.1.
UniGeneStr.43472.

3D structure databases

ProteinModelPortalQ28C91.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING8364.ENSXETP00000023285.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSXETT00000064480; ENSXETP00000061979; ENSXETG00000010628.
GeneID496886.
KEGGxtr:496886.

Organism-specific databases

CTD55862.
XenbaseXB-GENE-958554. echdc1.

Phylogenomic databases

GeneTreeENSGT00720000108837.
HOGENOMHOG000007808.
HOVERGENHBG054783.
OMAHKHMGLV.
OrthoDBEOG79W95T.
TreeFamTF315986.

Gene expression databases

BgeeQ28C91.

Family and domain databases

InterProIPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamPF00378. ECH. 1 hit.
[Graphical view]
PROSITEPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameECHD1_XENTR
AccessionPrimary (citable) accession number: Q28C91
Secondary accession number(s): F6UNG1, Q0VFD0, Q5M791
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: April 4, 2006
Last modified: February 19, 2014
This is version 50 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