Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable methylmalonyl-CoA mutase, mitochondrial

Gene

mmcm-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi618Cobalt (cobalamin axial ligand)By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Cobalamin, Cobalt, Metal-binding

Enzyme and pathway databases

ReactomeiR-CEL-196741. Cobalamin (Cbl, vitamin B12) transport and metabolism.
R-CEL-71032. Propionyl-CoA catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable methylmalonyl-CoA mutase, mitochondrial (EC:5.4.99.2)
Alternative name(s):
MethylmalonylCoA mutase homolog 1
Short name:
MCM
Gene namesi
Name:mmcm-1
ORF Names:ZK1058.1
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiZK1058.1; CE30404; WBGene00014202; mmcm-1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000019297? – 744Probable methylmalonyl-CoA mutase, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

EPDiQ23381.
PaxDbiQ23381.
PeptideAtlasiQ23381.
PRIDEiQ23381.

Expressioni

Gene expression databases

BgeeiWBGene00014202.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi40741. 1 interactor.
MINTiMINT-1062924.
STRINGi6239.ZK1058.1.1.

Structurei

3D structure databases

ProteinModelPortaliQ23381.
SMRiQ23381.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini605 – 737B12-bindingPROSITE-ProRule annotationAdd BLAST133

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IE7I. Eukaryota.
COG1884. LUCA.
COG2185. LUCA.
GeneTreeiENSGT00390000011892.
HOGENOMiHOG000003917.
InParanoidiQ23381.
KOiK01847.
OMAiGVNKYRP.
OrthoDBiEOG091G02GM.
PhylomeDBiQ23381.

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.

Q23381-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYLQLLKPTL LRCSTRPSSS GAYTRSPIDQ KWAAMAKKAM KGREADTLTW
60 70 80 90 100
NTPEGIPIKP LYLRSDRDCD AQRSVELPGQ FPFTRGPYPT MYTQRPWTIR
110 120 130 140 150
QYAGFSTVEE SNKFYKENIK AGQQGLSVAF DLATHRGYDS DNPRVFGDVG
160 170 180 190 200
MAGVAVDSVE DMRQLFDGIN LEKMSVSMTM NGAVVPVLAM YVVAAEEAGV
210 220 230 240 250
SRKLLAGTIQ NDILKEFMVR NTYIYPPEPS MRIIGDIFAY TSREMPKFNS
260 270 280 290 300
ISISGYHMQE AGADAVLEMA FTIADGIQYC ETGLNAGLTI DAFAPRLSFF
310 320 330 340 350
WGISMNFYME IAKMRAARRL WANLIKERFS PKSDKSMMLR THSQTSGWSL
360 370 380 390 400
TEQDPYNNII RTTIEAMASV FGGTQSLHTN SFDEALGLPT KFSARIARNT
410 420 430 440 450
QIIIQEESGI CNVADPWGGS YMMESLTDEI YEKALAVIKE IDELGGMAKA
460 470 480 490 500
VASGMTKLKI EEAAAKKQAR IDAGKDVIVG VNKYRLDHEQ QVEVLKIDNA
510 520 530 540 550
KVREEQCAKL NHIRATRDAE KAQKALDAIT EGARGNGNLM ELAIEAARAR
560 570 580 590 600
CTVGEISDAM EKVFNRHAAV NRLVSGAYKS EFGETSEMSQ VLERVKSFAD
610 620 630 640 650
RDGRQPRIMV AKMGQDGHDR GAKVIATGFA DLGFDVDVGP LFQTPLEAAQ
660 670 680 690 700
QAVDADVHVI GASSLAAGHL TLIPQLIGEL KKLGRPDILV VAGGVIPPQD
710 720 730 740
YKELYDAGVA LVFGPGTRLP ACANQILEKL EANLPEAPGK AASR
Length:744
Mass (Da):81,683
Last modified:June 20, 2002 - v2
Checksum:i599E22008D8FBAEC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35604 Genomic DNA. Translation: CAA84676.2.
PIRiT27674.
RefSeqiNP_497786.2. NM_065385.6.
UniGeneiCel.17830.

Genome annotation databases

EnsemblMetazoaiZK1058.1; ZK1058.1; WBGene00014202.
GeneIDi175503.
KEGGicel:CELE_ZK1058.1.
UCSCiZK1058.1.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35604 Genomic DNA. Translation: CAA84676.2.
PIRiT27674.
RefSeqiNP_497786.2. NM_065385.6.
UniGeneiCel.17830.

3D structure databases

ProteinModelPortaliQ23381.
SMRiQ23381.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi40741. 1 interactor.
MINTiMINT-1062924.
STRINGi6239.ZK1058.1.1.

Proteomic databases

EPDiQ23381.
PaxDbiQ23381.
PeptideAtlasiQ23381.
PRIDEiQ23381.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiZK1058.1; ZK1058.1; WBGene00014202.
GeneIDi175503.
KEGGicel:CELE_ZK1058.1.
UCSCiZK1058.1.1. c. elegans.

Organism-specific databases

CTDi175503.
WormBaseiZK1058.1; CE30404; WBGene00014202; mmcm-1.

Phylogenomic databases

eggNOGiENOG410IE7I. Eukaryota.
COG1884. LUCA.
COG2185. LUCA.
GeneTreeiENSGT00390000011892.
HOGENOMiHOG000003917.
InParanoidiQ23381.
KOiK01847.
OMAiGVNKYRP.
OrthoDBiEOG091G02GM.
PhylomeDBiQ23381.

Enzyme and pathway databases

ReactomeiR-CEL-196741. Cobalamin (Cbl, vitamin B12) transport and metabolism.
R-CEL-71032. Propionyl-CoA catabolism.

Miscellaneous databases

PROiQ23381.

Gene expression databases

BgeeiWBGene00014202.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiMUTA_CAEEL
AccessioniPrimary (citable) accession number: Q23381
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 20, 2002
Last modified: November 2, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  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.