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Protein

Ethylmalonyl-CoA decarboxylase

Gene

Echdc1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

(S)-ethylmalonyl-CoA = butanoyl-CoA + CO2.1 Publication
(S)-methylmalonyl-CoA = propanoyl-CoA + CO2.1 Publication

Kineticsi

  1. KM=0.96 µM for (S)-ethylmalonyl-CoA (in presence of 0 mM of ATP)1 Publication
  2. KM=6.5 µM for (S)-ethylmalonyl-CoA (in presence of 5 mM of ATP)1 Publication
  3. KM=3.1 µM for (S)-methylmalonyl-CoA (in presence of 0 mM of ATP)1 Publication
  4. KM=15.1 µM for (S)-methylmalonyl-CoA (in presence of 5 mM of ATP)1 Publication

    GO - Molecular functioni

    • carboxy-lyase activity Source: UniProtKB
    • methylmalonyl-CoA decarboxylase activity Source: UniProtKB-EC

    GO - Biological processi

    • metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17103.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ethylmalonyl-CoA decarboxylase (EC:4.1.1.94)
    Alternative name(s):
    Enoyl-CoA hydratase domain-containing protein 1
    Methylmalonyl-CoA decarboxylase (EC:4.1.1.41)
    Short name:
    MMCD
    Gene namesi
    Name:Echdc1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589 Componenti: Chromosome 10

    Organism-specific databases

    MGIiMGI:1277169. Echdc1.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • extracellular exosome Source: MGI
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 322322Ethylmalonyl-CoA decarboxylasePRO_0000273247Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei232 – 2321N6-acetyllysine; alternate1 Publication
    Modified residuei232 – 2321N6-succinyllysine; alternate1 Publication
    Modified residuei316 – 3161N6-succinyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9D9V3.
    PaxDbiQ9D9V3.
    PRIDEiQ9D9V3.

    PTM databases

    PhosphoSiteiQ9D9V3.

    Expressioni

    Gene expression databases

    BgeeiQ9D9V3.
    CleanExiMM_ECHDC1.
    ExpressionAtlasiQ9D9V3. baseline and differential.
    GenevisibleiQ9D9V3. MM.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-1858949.
    STRINGi10090.ENSMUSP00000020034.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D9V3.
    SMRiQ9D9V3. Positions 72-321.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1024.
    GeneTreeiENSGT00760000119100.
    HOGENOMiHOG000007808.
    HOVERGENiHBG054783.
    InParanoidiQ9D9V3.
    KOiK18426.
    OMAiHKHMGLV.
    OrthoDBiEOG79W95T.
    PhylomeDBiQ9D9V3.
    TreeFamiTF315986.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    InterProiIPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    [Graphical view]
    PfamiPF00378. ECH. 1 hit.
    [Graphical view]
    SUPFAMiSSF52096. SSF52096. 1 hit.
    PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9D9V3-1) [UniParc]FASTAAdd to basket

    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.

    « Hide

            10         20         30         40         50
    MRRCEVNSKP ISEYFGIPCE NREMAKCLLT SSLSVRTKLL QTGVSLYNTS
    60 70 80 90 100
    HGFHEEEVKK ILEQFPGGSI DLLKKQNGIG ILTLNNPNKM NAFSGVMMLQ
    110 120 130 140 150
    LLERVIELEN WTEGKGLIIH GAKNTFCSGS DLNAVKALST PESGVALSMF
    160 170 180 190 200
    MQNTLTRFMR LPLISVALVQ GWAMGGGAEL TTACDFRLMT EESVIRFVHK
    210 220 230 240 250
    EMGIVPSWGG TSRLVEIIGS RQALKVLSGT LKLDSKEALN IGLTDEVLQP
    260 270 280 290 300
    SDETTALEQA QEWLEKFVSG PPQVIRGLKK SVCSARELYI EEALQNERDV
    310 320
    LETLWGGPAN LEAIAKKGKH TK
    Length:322
    Mass (Da):35,467
    Last modified:March 1, 2003 - v2
    Checksum:iB25E26FEF0611EB1
    GO
    Isoform 2 (identifier: Q9D9V3-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-23: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:299
    Mass (Da):32,727
    Checksum:i8C08C7357BA365A6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21R → K in BAC26112 (PubMed:16141072).Curated
    Sequence conflicti4 – 41C → F in BAE26268 (PubMed:16141072).Curated
    Sequence conflicti22 – 221R → Q in BAC26112 (PubMed:16141072).Curated
    Sequence conflicti280 – 2801K → Q in BAE26268 (PubMed:16141072).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2323Missing in isoform 2. 1 PublicationVSP_022499Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    CCDSiCCDS23760.1. [Q9D9V3-1]
    CCDS48528.1. [Q9D9V3-2]
    RefSeqiNP_001103665.1. NM_001110195.1. [Q9D9V3-2]
    NP_080131.4. NM_025855.4. [Q9D9V3-1]
    UniGeneiMm.28930.

    Genome annotation databases

    EnsembliENSMUST00000020034; ENSMUSP00000020034; ENSMUSG00000019883. [Q9D9V3-1]
    ENSMUST00000160399; ENSMUSP00000125553; ENSMUSG00000019883. [Q9D9V3-2]
    GeneIDi52665.
    KEGGimmu:52665.
    UCSCiuc007esw.2. mouse. [Q9D9V3-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    CCDSiCCDS23760.1. [Q9D9V3-1]
    CCDS48528.1. [Q9D9V3-2]
    RefSeqiNP_001103665.1. NM_001110195.1. [Q9D9V3-2]
    NP_080131.4. NM_025855.4. [Q9D9V3-1]
    UniGeneiMm.28930.

    3D structure databases

    ProteinModelPortaliQ9D9V3.
    SMRiQ9D9V3. Positions 72-321.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    MINTiMINT-1858949.
    STRINGi10090.ENSMUSP00000020034.

    PTM databases

    PhosphoSiteiQ9D9V3.

    Proteomic databases

    MaxQBiQ9D9V3.
    PaxDbiQ9D9V3.
    PRIDEiQ9D9V3.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000020034; ENSMUSP00000020034; ENSMUSG00000019883. [Q9D9V3-1]
    ENSMUST00000160399; ENSMUSP00000125553; ENSMUSG00000019883. [Q9D9V3-2]
    GeneIDi52665.
    KEGGimmu:52665.
    UCSCiuc007esw.2. mouse. [Q9D9V3-1]

    Organism-specific databases

    CTDi55862.
    MGIiMGI:1277169. Echdc1.

    Phylogenomic databases

    eggNOGiCOG1024.
    GeneTreeiENSGT00760000119100.
    HOGENOMiHOG000007808.
    HOVERGENiHBG054783.
    InParanoidiQ9D9V3.
    KOiK18426.
    OMAiHKHMGLV.
    OrthoDBiEOG79W95T.
    PhylomeDBiQ9D9V3.
    TreeFamiTF315986.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17103.

    Miscellaneous databases

    ChiTaRSiEchdc1. mouse.
    NextBioi309291.
    PROiQ9D9V3.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9D9V3.
    CleanExiMM_ECHDC1.
    ExpressionAtlasiQ9D9V3. baseline and differential.
    GenevisibleiQ9D9V3. MM.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    InterProiIPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    [Graphical view]
    PfamiPF00378. ECH. 1 hit.
    [Graphical view]
    SUPFAMiSSF52096. SSF52096. 1 hit.
    PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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.
      , 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. 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.

    Entry informationi

    Entry nameiECHD1_MOUSE
    AccessioniPrimary (citable) accession number: Q9D9V3
    Secondary accession number(s): Q3U8C0
    , Q3UM30, Q8C185, Q9CTC5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: March 1, 2003
    Last modified: June 24, 2015
    This is version 103 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.