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Protein

Methylmalonyl-CoA epimerase, mitochondrial

Gene

MCEE

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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 bindingi50 – 501Cobalt; via tele nitrogen1 Publication
Metal bindingi122 – 1221Cobalt; via tele nitrogen1 Publication
Metal bindingi172 – 1721Cobalt1 Publication

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • methylmalonyl-CoA epimerase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Cobalt, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS13124-MONOMER.
BRENDAi5.1.99.1. 2681.
ReactomeiREACT_993. 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:16732. MCEE.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Methylmalonyl-CoA epimerase deficiency (MCEED)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAutosomal 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.

See also OMIM:251120

Organism-specific databases

MIMi251120. phenotype.
Orphaneti308425. Methylmalonic acidemia due to methylmalonyl-CoA epimerase deficiency.
PharmGKBiPA30683.

Polymorphism and mutation databases

BioMutaiMCEE.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3636MitochondrionSequence AnalysisAdd
BLAST
Chaini37 – 176140Methylmalonyl-CoA epimerase, mitochondrialPRO_0000012283Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141N6-succinyllysineBy similarity
Modified residuei150 – 1501N6-acetyllysine; alternateBy similarity
Modified residuei150 – 1501N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ96PE7.
PaxDbiQ96PE7.
PRIDEiQ96PE7.

2D gel databases

UCD-2DPAGEQ96PE7.

PTM databases

PhosphoSiteiQ96PE7.

Expressioni

Gene expression databases

BgeeiQ96PE7.
CleanExiHS_MCEE.
ExpressionAtlasiQ96PE7. baseline and differential.
GenevisibleiQ96PE7. HS.

Organism-specific databases

HPAiHPA035196.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
AGTRAPQ6RW133EBI-10292326,EBI-741181
CMTM5Q96DZ93EBI-10292326,EBI-2548702

Protein-protein interaction databases

BioGridi124208. 3 interactions.
IntActiQ96PE7. 2 interactions.
STRINGi9606.ENSP00000244217.

Structurei

Secondary structure

1
176
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi45 – 5410Combined sources
Helixi58 – 6710Combined sources
Beta strandi77 – 793Combined sources
Helixi80 – 823Combined sources
Beta strandi84 – 907Combined sources
Beta strandi92 – 10110Combined sources
Helixi109 – 1146Combined sources
Beta strandi119 – 12810Combined sources
Helixi130 – 13910Combined sources
Beta strandi155 – 1617Combined sources
Beta strandi171 – 1755Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RMUX-ray1.80A/B/C/D45-176[»]
ProteinModelPortaliQ96PE7.
SMRiQ96PE7. Positions 45-176.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi138 – 1414Poly-Lys

Sequence similaritiesi

Belongs to the glyoxalase I family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0346.
GeneTreeiENSGT00390000004772.
HOGENOMiHOG000232024.
HOVERGENiHBG052426.
InParanoidiQ96PE7.
KOiK05606.
OMAiRIDHIGI.
PhylomeDBiQ96PE7.
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.

Q96PE7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARVLKAAAA NAVGLFSRLQ APIPTVRASS TSQPLDQVTG SVWNLGRLNH
60 70 80 90 100
VAIAVPDLEK AAAFYKNILG AQVSEAVPLP EHGVSVVFVN LGNTKMELLH
110 120 130 140 150
PLGRDSPIAG FLQKNKAGGM HHICIEVDNI NAAVMDLKKK KIRSLSEEVK
160 170
IGAHGKPVIF LHPKDCGGVL VELEQA
Length:176
Mass (Da):18,749
Last modified:December 1, 2001 - v1
Checksum:iF783E5DF5D778220
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti76 – 761A → V.
Corresponds to variant rs11541017 [ dbSNP | Ensembl ].
VAR_049248
Natural varianti104 – 1041R → L.1 Publication
Corresponds to variant rs6748672 [ dbSNP | Ensembl ].
VAR_019511

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF364547 mRNA. Translation: AAK52052.1.
AC007881 Genomic DNA. Translation: AAY14749.1.
CH471053 Genomic DNA. Translation: EAW99778.1.
BC020825 mRNA. Translation: AAH20825.1.
CCDSiCCDS1915.1.
RefSeqiNP_115990.3. NM_032601.3.
UniGeneiHs.94949.

Genome annotation databases

EnsembliENST00000244217; ENSP00000244217; ENSG00000124370.
GeneIDi84693.
KEGGihsa:84693.
UCSCiuc002shs.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF364547 mRNA. Translation: AAK52052.1.
AC007881 Genomic DNA. Translation: AAY14749.1.
CH471053 Genomic DNA. Translation: EAW99778.1.
BC020825 mRNA. Translation: AAH20825.1.
CCDSiCCDS1915.1.
RefSeqiNP_115990.3. NM_032601.3.
UniGeneiHs.94949.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RMUX-ray1.80A/B/C/D45-176[»]
ProteinModelPortaliQ96PE7.
SMRiQ96PE7. Positions 45-176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124208. 3 interactions.
IntActiQ96PE7. 2 interactions.
STRINGi9606.ENSP00000244217.

PTM databases

PhosphoSiteiQ96PE7.

Polymorphism and mutation databases

BioMutaiMCEE.

2D gel databases

UCD-2DPAGEQ96PE7.

Proteomic databases

MaxQBiQ96PE7.
PaxDbiQ96PE7.
PRIDEiQ96PE7.

Protocols and materials databases

DNASUi84693.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000244217; ENSP00000244217; ENSG00000124370.
GeneIDi84693.
KEGGihsa:84693.
UCSCiuc002shs.2. human.

Organism-specific databases

CTDi84693.
GeneCardsiGC02M071336.
GeneReviewsiMCEE.
HGNCiHGNC:16732. MCEE.
HPAiHPA035196.
MIMi251120. phenotype.
608419. gene.
neXtProtiNX_Q96PE7.
Orphaneti308425. Methylmalonic acidemia due to methylmalonyl-CoA epimerase deficiency.
PharmGKBiPA30683.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0346.
GeneTreeiENSGT00390000004772.
HOGENOMiHOG000232024.
HOVERGENiHBG052426.
InParanoidiQ96PE7.
KOiK05606.
OMAiRIDHIGI.
PhylomeDBiQ96PE7.
TreeFamiTF313417.

Enzyme and pathway databases

BioCyciMetaCyc:HS13124-MONOMER.
BRENDAi5.1.99.1. 2681.
ReactomeiREACT_993. Propionyl-CoA catabolism.

Miscellaneous databases

ChiTaRSiMCEE. human.
GenomeRNAii84693.
NextBioi74761.
PROiQ96PE7.
SOURCEiSearch...

Gene expression databases

BgeeiQ96PE7.
CleanExiHS_MCEE.
ExpressionAtlasiQ96PE7. baseline and differential.
GenevisibleiQ96PE7. HS.

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

« Hide 'large scale' publications
  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.
    , 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. 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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "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.

Entry informationi

Entry nameiMCEE_HUMAN
AccessioniPrimary (citable) accession number: Q96PE7
Secondary accession number(s): Q53TP1, Q8WW63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: December 1, 2001
Last modified: June 24, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.