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Q9D9V3

- ECHD1_MOUSE

UniProt

Q9D9V3 - ECHD1_MOUSE

Protein

Ethylmalonyl-CoA decarboxylase

Gene

Echdc1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 2 (01 Mar 2003)
      Previous versions | rss
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    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

    1. carboxy-lyase activity Source: UniProtKB
    2. methylmalonyl-CoA decarboxylase activity Source: UniProtKB-EC

    GO - Biological processi

    1. metabolic process Source: UniProtKB

    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: Chromosome 10

    Organism-specific databases

    MGIiMGI:1277169. Echdc1.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    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

    ArrayExpressiQ9D9V3.
    BgeeiQ9D9V3.
    CleanExiMM_ECHDC1.
    GenevestigatoriQ9D9V3.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-1858949.

    Structurei

    3D structure databases

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

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1024.
    GeneTreeiENSGT00720000108837.
    HOGENOMiHOG000007808.
    HOVERGENiHBG054783.
    InParanoidiQ9D9V3.
    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. Align

    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

    MRRCEVNSKP ISEYFGIPCE NREMAKCLLT SSLSVRTKLL QTGVSLYNTS    50
    HGFHEEEVKK ILEQFPGGSI DLLKKQNGIG ILTLNNPNKM NAFSGVMMLQ 100
    LLERVIELEN WTEGKGLIIH GAKNTFCSGS DLNAVKALST PESGVALSMF 150
    MQNTLTRFMR LPLISVALVQ GWAMGGGAEL TTACDFRLMT EESVIRFVHK 200
    EMGIVPSWGG TSRLVEIIGS RQALKVLSGT LKLDSKEALN IGLTDEVLQP 250
    SDETTALEQA QEWLEKFVSG PPQVIRGLKK SVCSARELYI EEALQNERDV 300
    LETLWGGPAN LEAIAKKGKH TK 322
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS23760.1. [Q9D9V3-1 ]
    CCDS48528.1. [Q9D9V3-2 ]
    RefSeqi NP_001103665.1. NM_001110195.1. [Q9D9V3-2 ]
    NP_080131.4. NM_025855.4. [Q9D9V3-1 ]
    UniGenei Mm.28930.

    3D structure databases

    ProteinModelPortali Q9D9V3.
    SMRi Q9D9V3. Positions 72-321.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1858949.

    PTM databases

    PhosphoSitei Q9D9V3.

    Proteomic databases

    MaxQBi Q9D9V3.
    PaxDbi Q9D9V3.
    PRIDEi Q9D9V3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020034 ; ENSMUSP00000020034 ; ENSMUSG00000019883 . [Q9D9V3-1 ]
    ENSMUST00000160399 ; ENSMUSP00000125553 ; ENSMUSG00000019883 . [Q9D9V3-2 ]
    GeneIDi 52665.
    KEGGi mmu:52665.
    UCSCi uc007esw.2. mouse. [Q9D9V3-1 ]

    Organism-specific databases

    CTDi 55862.
    MGIi MGI:1277169. Echdc1.

    Phylogenomic databases

    eggNOGi COG1024.
    GeneTreei ENSGT00720000108837.
    HOGENOMi HOG000007808.
    HOVERGENi HBG054783.
    InParanoidi Q9D9V3.
    OMAi HKHMGLV.
    OrthoDBi EOG79W95T.
    PhylomeDBi Q9D9V3.
    TreeFami TF315986.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-17103.

    Miscellaneous databases

    NextBioi 309291.
    PROi Q9D9V3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9D9V3.
    Bgeei Q9D9V3.
    CleanExi MM_ECHDC1.
    Genevestigatori Q9D9V3.

    Family and domain databases

    Gene3Di 3.90.226.10. 1 hit.
    InterProi IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    [Graphical view ]
    Pfami PF00378. ECH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52096. SSF52096. 1 hit.
    PROSITEi PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 97 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