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P16332

- MUTA_MOUSE

UniProt

P16332 - MUTA_MOUSE

Protein

Methylmalonyl-CoA mutase, mitochondrial

Gene

Mut

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Involved in the degradation of several amino acids, odd-chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle.By similarity

    Catalytic activityi

    (R)-methylmalonyl-CoA = succinyl-CoA.

    Cofactori

    Adenosylcobalamin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi625 – 6251Cobalt (cobalamin axial ligand)By similarity

    GO - Molecular functioni

    1. cobalamin binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. methylmalonyl-CoA mutase activity Source: MGI
    4. modified amino acid binding Source: Ensembl

    GO - Biological processi

    1. homocysteine metabolic process Source: Ensembl
    2. post-embryonic development Source: MGI

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Cobalamin, Cobalt, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_189075. Defective MMAA causes methylmalonic aciduria type cblA.
    REACT_189097. Defective MUT causes methylmalonic aciduria mut type.
    REACT_189118. Cobalamin (Cbl, vitamin B12) transport and metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methylmalonyl-CoA mutase, mitochondrial (EC:5.4.99.2)
    Short name:
    MCM
    Alternative name(s):
    Methylmalonyl-CoA isomerase
    Gene namesi
    Name:Mut
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:97239. Mut.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3030MitochondrionBy similarityAdd
    BLAST
    Chaini31 – 748718Methylmalonyl-CoA mutase, mitochondrialPRO_0000019295Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei87 – 871N6-acetyllysine1 Publication
    Modified residuei210 – 2101N6-acetyllysine1 Publication
    Modified residuei333 – 3331N6-acetyllysine1 Publication
    Modified residuei341 – 3411N6-succinyllysine1 Publication
    Modified residuei593 – 5931N6-succinyllysine1 Publication
    Modified residuei600 – 6001N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP16332.
    PaxDbiP16332.
    PRIDEiP16332.

    PTM databases

    PhosphoSiteiP16332.

    Expressioni

    Gene expression databases

    ArrayExpressiP16332.
    BgeeiP16332.
    CleanExiMM_MUT.
    GenevestigatoriP16332.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    IntActiP16332. 2 interactions.
    MINTiMINT-4102615.

    Structurei

    3D structure databases

    ProteinModelPortaliP16332.
    SMRiP16332. Positions 34-747.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini612 – 744133B12-bindingPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the methylmalonyl-CoA mutase family.Curated
    Contains 1 B12-binding domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG2185.
    GeneTreeiENSGT00390000011892.
    HOGENOMiHOG000003917.
    HOVERGENiHBG006423.
    InParanoidiQ3UJU1.
    KOiK01847.
    OMAiSIYDMRQ.
    OrthoDBiEOG78PV8G.
    TreeFamiTF313557.

    Family and domain databases

    Gene3Di3.20.20.240. 1 hit.
    3.40.50.280. 1 hit.
    InterProiIPR006159. Acid_CoA_mut_C.
    IPR016176. Cbl-dep_enz_cat.
    IPR014348. Cbl-dep_enz_cat-sub.
    IPR006158. Cobalamin-bd.
    IPR006099. MeMalonylCoA_mutase_a/b_cat.
    IPR006098. MMCoA_mutase_a_cat.
    [Graphical view]
    PfamiPF02310. B12-binding. 1 hit.
    PF01642. MM_CoA_mutase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51703. SSF51703. 1 hit.
    SSF52242. SSF52242. 1 hit.
    TIGRFAMsiTIGR00640. acid_CoA_mut_C. 1 hit.
    TIGR00641. acid_CoA_mut_N. 1 hit.
    PROSITEiPS51332. B12_BINDING. 1 hit.
    PS00544. METMALONYL_COA_MUTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P16332-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRAKNQLFL LSPHYLKQLN IPSASRWKRL LHQQQPLHPE WAVLAKKQLK    50
    GKNPEDLIWH TPEGISIKPL YSRADTLDLP EELPGVKPFT RGPYPTMYTY 100
    RPWTIRQYAG FSTVEESNKF YKDNIKAGQQ GLSVAFDLAT HRGYDSDNPR 150
    VRGDVGMAGV AIDTVEDTKI LFDGIPLEKM SVSMTMNGAV IPVLATFIVT 200
    GEEQGVPKEK LTGTIQNDIL KEFMVRNTYI FPPEPSMKII ADIFQYTAQH 250
    MPKFNSISIS GYHMQEAGAD AILELAYTIA DGLEYCRTGL QAGLTIDEFA 300
    PRLSFFWGIG MNFYMEIAKM RAGRRLWAHL IEKMFQPKNS KSLLLRAHCQ 350
    TSGWSLTEQD PYNNIVRTAI EAMAAVFGGT QSLHTNSFDE ALGLPTVKSA 400
    RIARNTQIII QEESGIPKVA DPWGGSYMME SLTNDVYEAA LKLIYEVEEM 450
    GGMAKAVAEG IPKLRIEECA ARRQARIDSG SEVIVGVNKY QLEKEDSVEV 500
    LAIDNTSVRK KQIEKLKKIK SSRDQALAEQ CLSALTQCAA SGDGNILALA 550
    VDAARARCTV GEITDALKKV FGEHKANDRM VSGAYRQEFG ESKEITSAIK 600
    RVNKFMEREG RRPRLLVAKM GQDGHDRGAK VIATGFADLG FDVDIGPLFQ 650
    TPREVAQQAV DADVHAVGVS TLAAGHKTLV PELIKELTAL GRPDILVMCG 700
    GVIPPQDYEF LYEVGVSNVF GPGTRIPRAA VQVLDDIEKC LAEKQQSV 748
    Length:748
    Mass (Da):82,844
    Last modified:July 27, 2011 - v2
    Checksum:iDF4A62100A8BD743
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti256 – 2561S → P in CAA36204. (PubMed:1978672)Curated
    Sequence conflicti269 – 2691A → T in CAA36204. (PubMed:1978672)Curated
    Sequence conflicti385 – 3851T → S in CAA36204. (PubMed:1978672)Curated
    Sequence conflicti407 – 4071Q → R in CAA36204. (PubMed:1978672)Curated
    Sequence conflicti491 – 4911Q → H in CAA36204. (PubMed:1978672)Curated
    Sequence conflicti499 – 50810EVLAIDNTSV → HLLAIDIISL in CAA36204. (PubMed:1978672)Curated
    Sequence conflicti561 – 5611G → P in CAA36204. (PubMed:1978672)Curated
    Sequence conflicti567 – 5671L → F in CAA36204. (PubMed:1978672)Curated
    Sequence conflicti613 – 6142PR → LG in CAA36204. (PubMed:1978672)Curated
    Sequence conflicti622 – 6221Q → K in CAA36204. (PubMed:1978672)Curated
    Sequence conflicti657 – 6582QQ → HD in CAA36204. (PubMed:1978672)Curated
    Sequence conflicti672 – 6721L → H in CAA36204. (PubMed:1978672)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51941 mRNA. Translation: CAA36204.1.
    AK146309 mRNA. Translation: BAE27064.1.
    CH466559 Genomic DNA. Translation: EDL23389.1.
    CCDSiCCDS37618.1.
    PIRiS08680.
    RefSeqiNP_032676.2. NM_008650.3.
    UniGeneiMm.259884.

    Genome annotation databases

    EnsembliENSMUST00000169611; ENSMUSP00000130941; ENSMUSG00000023921.
    GeneIDi17850.
    KEGGimmu:17850.
    UCSCiuc008coo.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51941 mRNA. Translation: CAA36204.1 .
    AK146309 mRNA. Translation: BAE27064.1 .
    CH466559 Genomic DNA. Translation: EDL23389.1 .
    CCDSi CCDS37618.1.
    PIRi S08680.
    RefSeqi NP_032676.2. NM_008650.3.
    UniGenei Mm.259884.

    3D structure databases

    ProteinModelPortali P16332.
    SMRi P16332. Positions 34-747.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P16332. 2 interactions.
    MINTi MINT-4102615.

    PTM databases

    PhosphoSitei P16332.

    Proteomic databases

    MaxQBi P16332.
    PaxDbi P16332.
    PRIDEi P16332.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000169611 ; ENSMUSP00000130941 ; ENSMUSG00000023921 .
    GeneIDi 17850.
    KEGGi mmu:17850.
    UCSCi uc008coo.2. mouse.

    Organism-specific databases

    CTDi 4594.
    MGIi MGI:97239. Mut.

    Phylogenomic databases

    eggNOGi COG2185.
    GeneTreei ENSGT00390000011892.
    HOGENOMi HOG000003917.
    HOVERGENi HBG006423.
    InParanoidi Q3UJU1.
    KOi K01847.
    OMAi SIYDMRQ.
    OrthoDBi EOG78PV8G.
    TreeFami TF313557.

    Enzyme and pathway databases

    Reactomei REACT_189075. Defective MMAA causes methylmalonic aciduria type cblA.
    REACT_189097. Defective MUT causes methylmalonic aciduria mut type.
    REACT_189118. Cobalamin (Cbl, vitamin B12) transport and metabolism.

    Miscellaneous databases

    ChiTaRSi MUT. mouse.
    NextBioi 292593.
    PROi P16332.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16332.
    Bgeei P16332.
    CleanExi MM_MUT.
    Genevestigatori P16332.

    Family and domain databases

    Gene3Di 3.20.20.240. 1 hit.
    3.40.50.280. 1 hit.
    InterProi IPR006159. Acid_CoA_mut_C.
    IPR016176. Cbl-dep_enz_cat.
    IPR014348. Cbl-dep_enz_cat-sub.
    IPR006158. Cobalamin-bd.
    IPR006099. MeMalonylCoA_mutase_a/b_cat.
    IPR006098. MMCoA_mutase_a_cat.
    [Graphical view ]
    Pfami PF02310. B12-binding. 1 hit.
    PF01642. MM_CoA_mutase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51703. SSF51703. 1 hit.
    SSF52242. SSF52242. 1 hit.
    TIGRFAMsi TIGR00640. acid_CoA_mut_C. 1 hit.
    TIGR00641. acid_CoA_mut_N. 1 hit.
    PROSITEi PS51332. B12_BINDING. 1 hit.
    PS00544. METMALONYL_COA_MUTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure and activity of mouse methylmalonyl-CoA mutase."
      Wilkemeyer M.F., Crane A.M., Ledley F.D.
      Biochem. J. 271:449-455(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "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].
      Strain: BALB/c.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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-341 AND LYS-593, 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-87; LYS-210; LYS-333 AND LYS-600, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiMUTA_MOUSE
    AccessioniPrimary (citable) accession number: P16332
    Secondary accession number(s): Q3UJU1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 118 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