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Reviewed, UniProtKB/Swiss-Prot Q23381 (MUTA_CAEEL)

Last modified June 16, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable methylmalonyl-CoA mutase, mitochondrial
    EC=5.4.99.2
Alternative name(s):
    MethylmalonylCoA mutase homolog 1
      Short name=MCM
Gene names
Name: mmcm-1
ORF Names: ZK1058.1
OrganismCaenorhabditis elegans [Complete proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length744 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Involved, in man, in the degradation of several amino acids, odd-chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle. MCM has different functions in other species By similarity.

Catalytic activity

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

Cofactor

Adenosylcobalamin By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the methylmalonyl-CoA mutase family.

Contains 1 B12-binding domain.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandCobalamin
Cobalt
Metal-binding
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncobalamin binding

Inferred from electronic annotation. Source: UniProtKB-KW

cobalt ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

methylmalonyl-CoA mutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 744Probable methylmalonyl-CoA mutase, mitochondrialPRO_0000019297

Regions

Domain605 – 737133B12-binding

Sites

Metal binding6181Cobalt (cobalamin axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q23381-1 [UniParc].

Last modified June 20, 2002. Version 2.
Checksum: 599E22008D8FBAEC

FASTA74481,683
        10         20         30         40         50         60 
MYLQLLKPTL LRCSTRPSSS GAYTRSPIDQ KWAAMAKKAM KGREADTLTW NTPEGIPIKP 

        70         80         90        100        110        120 
LYLRSDRDCD AQRSVELPGQ FPFTRGPYPT MYTQRPWTIR QYAGFSTVEE SNKFYKENIK 

       130        140        150        160        170        180 
AGQQGLSVAF DLATHRGYDS DNPRVFGDVG MAGVAVDSVE DMRQLFDGIN LEKMSVSMTM 

       190        200        210        220        230        240 
NGAVVPVLAM YVVAAEEAGV SRKLLAGTIQ NDILKEFMVR NTYIYPPEPS MRIIGDIFAY 

       250        260        270        280        290        300 
TSREMPKFNS ISISGYHMQE AGADAVLEMA FTIADGIQYC ETGLNAGLTI DAFAPRLSFF 

       310        320        330        340        350        360 
WGISMNFYME IAKMRAARRL WANLIKERFS PKSDKSMMLR THSQTSGWSL TEQDPYNNII 

       370        380        390        400        410        420 
RTTIEAMASV FGGTQSLHTN SFDEALGLPT KFSARIARNT QIIIQEESGI CNVADPWGGS 

       430        440        450        460        470        480 
YMMESLTDEI YEKALAVIKE IDELGGMAKA VASGMTKLKI EEAAAKKQAR IDAGKDVIVG 

       490        500        510        520        530        540 
VNKYRLDHEQ QVEVLKIDNA KVREEQCAKL NHIRATRDAE KAQKALDAIT EGARGNGNLM 

       550        560        570        580        590        600 
ELAIEAARAR CTVGEISDAM EKVFNRHAAV NRLVSGAYKS EFGETSEMSQ VLERVKSFAD 

       610        620        630        640        650        660 
RDGRQPRIMV AKMGQDGHDR GAKVIATGFA DLGFDVDVGP LFQTPLEAAQ QAVDADVHVI 

       670        680        690        700        710        720 
GASSLAAGHL TLIPQLIGEL KKLGRPDILV VAGGVIPPQD YKELYDAGVA LVFGPGTRLP 

       730        740 
ACANQILEKL EANLPEAPGK AASR 

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References

[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.

Cross-references

Sequence databases

Z35604 Genomic DNA. Translation: CAA84676.2.
PIRT27674.
RefSeqNP_497786.2.
UniGeneCel.17830

3D structure databases

HSSPHSSP built from PDB template 1REQ based on UniProtKB P11653.
ModBaseSearch...

Protein-protein interaction databases

IntActQ23381. 1 interaction.

Genome annotation databases

EnsemblZK1058.1. Caenorhabditis elegans. [Contig view]
GeneID175503.
KEGGcel:ZK1058.1.

Organism-specific databases

WormBaseWBGene00014202. mmcm-1.
WormPepZK1058.1. CE30404. [WorfDB]

Phylogenomic databases

OMAQ23381. IDSGSEV.

Enzyme and pathway databases

BRENDA5.4.99.2. 672.

Gene expression databases

ArrayExpressQ23381.

Family and domain databases

InterProIPR006159. Acid_CoA_mut_C.
IPR014348. Cbl-dep_enz_cat-sub.
IPR006158. Cobalamin-bd.
IPR006099. MMCoA_mutase_a/b_cat.
IPR006098. MMCoA_mutase_a_cat.
[Graphical view]
Gene3DG3DSA:3.40.50.280. B12_bd. 1 hit.
G3DSA:3.20.20.240. Cobalamin-dep_enz_cat. 1 hit.
PfamPF02310. B12-binding. 1 hit.
PF01642. MM_CoA_mutase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00640. acid_CoA_mut_C. 1 hit.
TIGR00641. acid_CoA_mut_N. 1 hit.
PROSITEPS51332. B12_BINDING. 1 hit.
PS00544. METMALONYL_COA_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio888440.

Entry information

Entry nameMUTA_CAEEL
AccessionPrimary (citable) accession number: Q23381
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 20, 2002
Last modified: June 16, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents