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Q9D9V3 (ECHD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. 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·Alt products·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length322 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. Ref.3

Catalytic activity

(S)-ethylmalonyl-CoA = butanoyl-CoA + CO2. Ref.3

(S)-methylmalonyl-CoA = propanoyl-CoA + CO2. Ref.3

Subcellular location

Cytoplasmcytosol Probable Ref.3.

Sequence similarities

Belongs to the enoyl-CoA hydratase/isomerase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.96 µM for (S)-ethylmalonyl-CoA (in presence of 0 mM of ATP) Ref.3

KM=6.5 µM for (S)-ethylmalonyl-CoA (in presence of 5 mM of ATP)

KM=3.1 µM for (S)-methylmalonyl-CoA (in presence of 0 mM of ATP)

KM=15.1 µM for (S)-methylmalonyl-CoA (in presence of 5 mM of ATP)

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   Molecular functionLyase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmetabolic process

Inferred from direct assay Ref.3. Source: UniProtKB

   Cellular_componentcytosol

Inferred from direct assay Ref.3. Source: UniProtKB

   Molecular_functioncarboxy-lyase activity

Inferred from direct assay Ref.3. Source: UniProtKB

methylmalonyl-CoA decarboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9D9V3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9D9V3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 322322Ethylmalonyl-CoA decarboxylase
PRO_0000273247

Amino acid modifications

Modified residue2321N6-acetyllysine; alternate Ref.5
Modified residue2321N6-succinyllysine; alternate Ref.4
Modified residue3161N6-succinyllysine Ref.4

Natural variations

Alternative sequence1 – 2323Missing in isoform 2.
VSP_022499

Experimental info

Sequence conflict21R → K in BAC26112. Ref.1
Sequence conflict41C → F in BAE26268. Ref.1
Sequence conflict221R → Q in BAC26112. Ref.1
Sequence conflict2801K → Q in BAE26268. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 2.
Checksum: B25E26FEF0611EB1

FASTA32235,467
        10         20         30         40         50         60 
MRRCEVNSKP ISEYFGIPCE NREMAKCLLT SSLSVRTKLL QTGVSLYNTS HGFHEEEVKK 

        70         80         90        100        110        120 
ILEQFPGGSI DLLKKQNGIG ILTLNNPNKM NAFSGVMMLQ LLERVIELEN WTEGKGLIIH 

       130        140        150        160        170        180 
GAKNTFCSGS DLNAVKALST PESGVALSMF MQNTLTRFMR LPLISVALVQ GWAMGGGAEL 

       190        200        210        220        230        240 
TTACDFRLMT EESVIRFVHK EMGIVPSWGG TSRLVEIIGS RQALKVLSGT LKLDSKEALN 

       250        260        270        280        290        300 
IGLTDEVLQP SDETTALEQA QEWLEKFVSG PPQVIRGLKK SVCSARELYI EEALQNERDV 

       310        320 
LETLWGGPAN LEAIAKKGKH TK 

« Hide

Isoform 2 [UniParc].

Checksum: 8C08C7357BA365A6
Show »

FASTA29932,727

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Bone marrow, Mammary gland, Skin and Testis.
[2]"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] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Egg.
[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: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
[4]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-232 AND LYS-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK003965 mRNA. Translation: BAB23096.1.
AK006444 mRNA. Translation: BAB24592.2.
AK028775 mRNA. Translation: BAC26112.1.
AK145162 mRNA. Translation: BAE26268.1.
AK150932 mRNA. Translation: BAE29969.1.
AK152285 mRNA. Translation: BAE31098.1.
AK153454 mRNA. Translation: BAE32007.1.
AK166589 mRNA. Translation: BAE38876.1.
AK166634 mRNA. Translation: BAE38907.1.
AK166660 mRNA. Translation: BAE38924.1.
BC066183 mRNA. Translation: AAH66183.1.
CCDSCCDS23760.1. [Q9D9V3-1]
CCDS48528.1. [Q9D9V3-2]
RefSeqNP_001103665.1. NM_001110195.1. [Q9D9V3-2]
NP_080131.4. NM_025855.4. [Q9D9V3-1]
UniGeneMm.28930.

3D structure databases

ProteinModelPortalQ9D9V3.
SMRQ9D9V3. Positions 72-321.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1858949.

PTM databases

PhosphoSiteQ9D9V3.

Proteomic databases

MaxQBQ9D9V3.
PaxDbQ9D9V3.
PRIDEQ9D9V3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020034; ENSMUSP00000020034; ENSMUSG00000019883. [Q9D9V3-1]
ENSMUST00000160399; ENSMUSP00000125553; ENSMUSG00000019883. [Q9D9V3-2]
GeneID52665.
KEGGmmu:52665.
UCSCuc007esw.2. mouse. [Q9D9V3-1]

Organism-specific databases

CTD55862.
MGIMGI:1277169. Echdc1.

Phylogenomic databases

eggNOGCOG1024.
GeneTreeENSGT00720000108837.
HOGENOMHOG000007808.
HOVERGENHBG054783.
InParanoidQ9D9V3.
OMAHKHMGLV.
OrthoDBEOG79W95T.
PhylomeDBQ9D9V3.
TreeFamTF315986.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17103.

Gene expression databases

ArrayExpressQ9D9V3.
BgeeQ9D9V3.
CleanExMM_ECHDC1.
GenevestigatorQ9D9V3.

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

NextBio309291.
PROQ9D9V3.
SOURCESearch...

Entry information

Entry nameECHD1_MOUSE
AccessionPrimary (citable) accession number: Q9D9V3
Secondary accession number(s): Q3U8C0 expand/collapse secondary AC list , Q3UM30, Q8C185, Q9CTC5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 96 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot