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Protein

Methylmalonyl-CoA epimerase, mitochondrial

Gene

Mcee

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi52 – 521Cobalt; via tele nitrogenBy similarity
Metal bindingi124 – 1241Cobalt; via tele nitrogenBy similarity
Metal bindingi174 – 1741CobaltBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Cobalt, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-71032. Propionyl-CoA catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylmalonyl-CoA epimerase, mitochondrial (EC:5.1.99.1)
Alternative name(s):
DL-methylmalonyl-CoA racemase
Gene namesi
Name:Mcee
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1920974. Mcee.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3838MitochondrionSequence analysisAdd
BLAST
Chaini39 – 178140Methylmalonyl-CoA epimerase, mitochondrialPRO_0000012284Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei116 – 1161N6-succinyllysineCombined sources
Modified residuei152 – 1521N6-acetyllysine; alternateCombined sources
Modified residuei152 – 1521N6-succinyllysine; alternateCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9D1I5.
MaxQBiQ9D1I5.
PaxDbiQ9D1I5.
PRIDEiQ9D1I5.

PTM databases

iPTMnetiQ9D1I5.
PhosphoSiteiQ9D1I5.

Expressioni

Gene expression databases

BgeeiQ9D1I5.
CleanExiMM_MCEE.
GenevisibleiQ9D1I5. MM.

Interactioni

Protein-protein interaction databases

IntActiQ9D1I5. 1 interaction.
MINTiMINT-1860107.
STRINGi10090.ENSMUSP00000047855.

Structurei

3D structure databases

ProteinModelPortaliQ9D1I5.
SMRiQ9D1I5. Positions 47-178.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi140 – 1434Poly-Lys

Sequence similaritiesi

Belongs to the glyoxalase I family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2944. Eukaryota.
COG0346. LUCA.
GeneTreeiENSGT00390000004772.
HOGENOMiHOG000232024.
HOVERGENiHBG052426.
InParanoidiQ9D1I5.
KOiK05606.
OMAiIHHICYE.
OrthoDBiEOG7WQ7VF.
PhylomeDBiQ9D1I5.
TreeFamiTF313417.

Family and domain databases

Gene3Di3.10.180.10. 1 hit.
InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR017515. MeMalonyl-CoA_epimerase.
[Graphical view]
SUPFAMiSSF54593. SSF54593. 1 hit.
TIGRFAMsiTIGR03081. metmalonyl_epim. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9D1I5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRVVKAAAL AAGATGLFSR VQTSVAIGRS FSTPQSQFQE SSPVWKLGRL
60 70 80 90 100
NHVAVAVPDL EKASSFYRDV LGAQVSEVVP LPEHGVSVVF VNLGNTKMEL
110 120 130 140 150
LHPLGSDSPI TGFLQKNKAG GMHHVCIEVD NISAAVMDLK KKKIRSLSDE
160 170
AKIGAHGKPV IFLHPKDCGG VLVELEQA
Length:178
Mass (Da):19,017
Last modified:June 1, 2001 - v1
Checksum:i0A496AF10455D379
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003511 mRNA. Translation: BAB22828.1.
BC038157 mRNA. Translation: AAH38157.1.
CCDSiCCDS21334.1.
RefSeqiNP_082902.1. NM_028626.1.
UniGeneiMm.10093.

Genome annotation databases

EnsembliENSMUST00000037205; ENSMUSP00000047855; ENSMUSG00000033429.
GeneIDi73724.
KEGGimmu:73724.
UCSCiuc009hgi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003511 mRNA. Translation: BAB22828.1.
BC038157 mRNA. Translation: AAH38157.1.
CCDSiCCDS21334.1.
RefSeqiNP_082902.1. NM_028626.1.
UniGeneiMm.10093.

3D structure databases

ProteinModelPortaliQ9D1I5.
SMRiQ9D1I5. Positions 47-178.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D1I5. 1 interaction.
MINTiMINT-1860107.
STRINGi10090.ENSMUSP00000047855.

PTM databases

iPTMnetiQ9D1I5.
PhosphoSiteiQ9D1I5.

Proteomic databases

EPDiQ9D1I5.
MaxQBiQ9D1I5.
PaxDbiQ9D1I5.
PRIDEiQ9D1I5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000037205; ENSMUSP00000047855; ENSMUSG00000033429.
GeneIDi73724.
KEGGimmu:73724.
UCSCiuc009hgi.1. mouse.

Organism-specific databases

CTDi84693.
MGIiMGI:1920974. Mcee.

Phylogenomic databases

eggNOGiKOG2944. Eukaryota.
COG0346. LUCA.
GeneTreeiENSGT00390000004772.
HOGENOMiHOG000232024.
HOVERGENiHBG052426.
InParanoidiQ9D1I5.
KOiK05606.
OMAiIHHICYE.
OrthoDBiEOG7WQ7VF.
PhylomeDBiQ9D1I5.
TreeFamiTF313417.

Enzyme and pathway databases

ReactomeiR-MMU-71032. Propionyl-CoA catabolism.

Miscellaneous databases

ChiTaRSiMcee. mouse.
PROiQ9D1I5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D1I5.
CleanExiMM_MCEE.
GenevisibleiQ9D1I5. MM.

Family and domain databases

Gene3Di3.10.180.10. 1 hit.
InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR017515. MeMalonyl-CoA_epimerase.
[Graphical view]
SUPFAMiSSF54593. SSF54593. 1 hit.
TIGRFAMsiTIGR03081. metmalonyl_epim. 1 hit.
ProtoNetiSearch...

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].
    Strain: C57BL/6J.
    Tissue: Embryo.
  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].
    Tissue: Uterus.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung and Pancreas.
  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-116 AND LYS-152, 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-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMCEE_MOUSE
AccessioniPrimary (citable) accession number: Q9D1I5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 100 of the entry and version 1 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

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 one 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.