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Q96PE7 (MCEE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylmalonyl-CoA epimerase, mitochondrial

EC=5.1.99.1
Alternative name(s):
DL-methylmalonyl-CoA racemase
Gene names
Name:MCEE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length176 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Subcellular location

Mitochondrion Probable.

Involvement in disease

Methylmalonyl-CoA epimerase deficiency (MCEED) [MIM:251120]: Autosomal recessive inborn error of amino acid metabolism, involving valine, threonine, isoleucine and methionine. This organic aciduria may present in the neonatal period with life-threatening metabolic acidosis, hyperammonemia, feeding difficulties, pancytopenia and coma.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5

Sequence similarities

Belongs to the glyoxalase I family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3636Mitochondrion Potential
Chain37 – 176140Methylmalonyl-CoA epimerase, mitochondrial
PRO_0000012283

Regions

Compositional bias138 – 1414Poly-Lys

Sites

Metal binding501Cobalt; via tele nitrogen
Metal binding1221Cobalt; via tele nitrogen
Metal binding1721Cobalt

Amino acid modifications

Modified residue1141N6-succinyllysine By similarity
Modified residue1501N6-acetyllysine; alternate By similarity
Modified residue1501N6-succinyllysine; alternate By similarity

Natural variations

Natural variant761A → V.
Corresponds to variant rs11541017 [ dbSNP | Ensembl ].
VAR_049248
Natural variant1041R → L. Ref.4
Corresponds to variant rs6748672 [ dbSNP | Ensembl ].
VAR_019511

Secondary structure

...................... 176
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96PE7 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: F783E5DF5D778220

FASTA17618,749
        10         20         30         40         50         60 
MARVLKAAAA NAVGLFSRLQ APIPTVRASS TSQPLDQVTG SVWNLGRLNH VAIAVPDLEK 

        70         80         90        100        110        120 
AAAFYKNILG AQVSEAVPLP EHGVSVVFVN LGNTKMELLH PLGRDSPIAG FLQKNKAGGM 

       130        140        150        160        170 
HHICIEVDNI NAAVMDLKKK KIRSLSEEVK IGAHGKPVIF LHPKDCGGVL VELEQA 

« Hide

References

« Hide 'large scale' references
[1]"Identification of the human methylmalonyl-CoA racemase gene based on the analysis of prokaryotic gene arrangements. Implications for decoding the human genome."
Bobik T.A., Rasche M.E.
J. Biol. Chem. 276:37194-37198(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Liver.
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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], VARIANT LEU-104.
Tissue: Liver.
[5]"A homozygous nonsense mutation in the methylmalonyl-CoA epimerase gene (MCEE) results in mild methylmalonic aciduria."
Bikker H., Bakker H.D., Abeling N.G.G.M., Poll-The B.T., Kleijer W.J., Rosenblatt D.S., Waterham H.R., Wanders R.J.A., Duran M.
Hum. Mutat. 27:640-643(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MCEED.
[6]"Crystal structure of human methylmalonyl-CoA epimerase, MCEE."
Structural genomics consortium (SGC)
Submitted (APR-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 45-176 IN COMPLEX WITH COBALT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF364547 mRNA. Translation: AAK52052.1.
AC007881 Genomic DNA. Translation: AAY14749.1.
CH471053 Genomic DNA. Translation: EAW99778.1.
BC020825 mRNA. Translation: AAH20825.1.
CCDSCCDS1915.1.
RefSeqNP_115990.3. NM_032601.3.
UniGeneHs.94949.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3RMUX-ray1.80A/B/C/D45-176[»]
ProteinModelPortalQ96PE7.
SMRQ96PE7. Positions 45-176.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124208. 1 interaction.
STRING9606.ENSP00000244217.

PTM databases

PhosphoSiteQ96PE7.

2D gel databases

UCD-2DPAGEQ96PE7.

Proteomic databases

MaxQBQ96PE7.
PaxDbQ96PE7.
PRIDEQ96PE7.

Protocols and materials databases

DNASU84693.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000244217; ENSP00000244217; ENSG00000124370.
GeneID84693.
KEGGhsa:84693.
UCSCuc002shs.2. human.

Organism-specific databases

CTD84693.
GeneCardsGC02M071336.
GeneReviewsMCEE.
HGNCHGNC:16732. MCEE.
HPAHPA035196.
MIM251120. phenotype.
608419. gene.
neXtProtNX_Q96PE7.
Orphanet308425. Methylmalonic acidemia due to methylmalonyl-CoA epimerase deficiency.
PharmGKBPA30683.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0346.
HOGENOMHOG000232024.
HOVERGENHBG052426.
InParanoidQ96PE7.
KOK05606.
OMAEKSPIAG.
PhylomeDBQ96PE7.
TreeFamTF313417.

Enzyme and pathway databases

BioCycMetaCyc:HS13124-MONOMER.
BRENDA5.1.99.1. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ96PE7.
BgeeQ96PE7.
CleanExHS_MCEE.
GenevestigatorQ96PE7.

Family and domain databases

Gene3D3.10.180.10. 1 hit.
InterProIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR017515. MeMalonyl-CoA_epimerase.
[Graphical view]
SUPFAMSSF54593. SSF54593. 1 hit.
TIGRFAMsTIGR03081. metmalonyl_epim. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi84693.
NextBio74761.
PROQ96PE7.
SOURCESearch...

Entry information

Entry nameMCEE_HUMAN
AccessionPrimary (citable) accession number: Q96PE7
Secondary accession number(s): Q53TP1, Q8WW63
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM