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Q59268 (MGM_EUBBA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
2-methyleneglutarate mutase

EC=5.4.99.4
Alternative name(s):
Alpha-methyleneglutarate mutase
Gene names
Name:mgm
OrganismEubacterium barkeri (Clostridium barkeri)
Taxonomic identifier1528 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesEubacteriaceaeEubacterium

Protein attributes

Sequence length614 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the fermentation of nicotinate to ammonia, propionate, acetate and carbon dioxide.

Catalytic activity

2-methyleneglutarate = 2-methylene-3-methylsuccinate. Ref.1 Ref.3 Ref.4 Ref.7

Cofactor

Cobalamin. Contains a mixture of adenosylcobalamin and oxygen-stable cob(II)alamin. Ref.1 Ref.3 Ref.5 Ref.6 Ref.7

Enzyme regulation

Inhibited by intrinsic factor and iodoacetic acid. Competitively inhibited by itaconate, mesaconate, succinate, 1-methyl-1,2-trans-clycopropane, dicarboxylate and L-malate. Non-competitively inhibited by glutaconate and 1-methyl-1,2-cis-cyclopropanedicarboxylate. Not inhibited by acrylate or by the chelating agents alpha,alpha-dipyridyl or EDTA. Not activated by Fe2+, Mg2+, Mn2+ or Ca2+. Unaffected by K+, Na+, NH4+, Rb+ or Li+. Ref.3 Ref.7

Pathway

Cofactor degradation; nicotinate degradation; propanoate and pyruvate from 6-hydroxynicotinate: step 5/8. Ref.2

Subunit structure

Homotetramer. Ref.4

Induction

By nicotinate. Ref.3 Ref.7

Sequence similarities

Contains 1 B12-binding domain.

Biophysicochemical properties

pH dependence:

Activity decreases rapidly below pH 7.5 in phosphate buffer, and below pH 8.0 in Tris buffer. Ref.3

Ontologies

Keywords
   LigandCobalamin
Cobalt
Metal-binding
   Molecular functionIsomerase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcofactor catabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_function2-methyleneglutarate mutase activity

Inferred from direct assay Ref.1. Source: UniProtKB

cobalamin binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6146142-methyleneglutarate mutase
PRO_0000096464

Regions

Domain472 – 614143B12-binding

Sites

Metal binding4851Cobalt (cobalamin axial ligand) By similarity

Experimental info

Mutagenesis4641H → Q: No effect on activity. Ref.7
Mutagenesis4831D → N: Activity reduced 2000-fold. Ref.7
Mutagenesis4851H → Q: Loss of activity. Ref.7
Sequence conflict971K → W AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q59268 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 37B78FEB06A4A3D1

FASTA61466,750
        10         20         30         40         50         60 
MQEKTKRIIK EDIEAVRAYS DCFDVEMPDL DENGEVIGLP APYPREVAGT VRSGYRIYDL 

        70         80         90        100        110        120 
AKKAKERGWP IQNPILGRNT AEETYGESQE MYAYADKFDE TLFHFVHAEA TRHIDPLKGR 

       130        140        150        160        170        180 
ELINQSRGKG GITPIGEREF IAMGGGSKHP VRINATGDTP HLSIINALIA GFDGTDIGPV 

       190        200        210        220        230        240 
IHVHFGGRGI HDYKTKVVNG YKAIQICAEN NIFVQLDSHK HLNNIGGTDG MALAMCLLSE 

       250        260        270        280        290        300 
GLAVHAGLPW ELSAIQMNVA GINIYADLAV MRAFRKACHS KSIIAVPETF QNPPGNLVAE 

       310        320        330        340        350        360 
AAHFSRMAVT AKLGGADFYR PKAAESVGIP TGDSMGQAIW GTEDVFGHVV NPDIQSPVID 

       370        380        390        400        410        420 
AREAEIIDEA LAVLEATLHL EGLTLEAMTD DFWKQWSDEA LIDLIVAAGK AGVLDSQRAA 

       430        440        450        460        470        480 
GWDLKRHVVV NRDKDGITRY VKGYTPLGVD ASRCAQSDED VEVHVEKAPT RPEKIVLATV 

       490        500        510        520        530        540 
GADAHVNGIN VIREAFQDAG YDVVYLRGMN LPESVAEVAA EVGADAVGVS NLLGLGMELF 

       550        560        570        580        590        600 
PRVSKRLEEL GLRDKMVVCA GGRIAEKEEE HRQFEEKIQK EGSAFMGMDG FFGPGSSPED 

       610 
CVKIIGDMIN AKKA 

« Hide

References

[1]"Cloning, sequencing and expression of the gene encoding the coenzyme B12-dependent 2-methyleneglutarate mutase from Clostridium barkeri in Escherichia coli."
Beatrix B., Zelder O., Linder D., Buckel W.
Eur. J. Biochem. 221:101-109(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21; 68-78; 79-103; 122-126; 141-145; 395-409; 494-507; 547-552 AND 564-576, CATALYTIC ACTIVITY, COFACTOR.
Strain: ATCC 25849 / DSM 1223 / JCM 1389 / NCIB 10623.
[2]"Molecular and functional analysis of nicotinate catabolism in Eubacterium barkeri."
Alhapel A., Darley D.J., Wagener N., Eckel E., Elsner N., Pierik A.J.
Proc. Natl. Acad. Sci. U.S.A. 103:12341-12346(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY.
Strain: ATCC 25849 / DSM 1223 / JCM 1389 / NCIB 10623.
[3]"Nicotinic acid metabolism. VI. Purification and properties of alpha-methyleneglutarate mutase (B 12-dependent) and methylitaconate isomerase."
Kung H.F., Stadtman T.C.
J. Biol. Chem. 246:3378-3388(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.
[4]"Assay and purification of the adenosylcobalamin-dependent 2-methyleneglutarate mutase from Clostridium barkeri."
Michel C., Hartrampf G., Buckel W.
Eur. J. Biochem. 184:103-107(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBUNIT.
[5]"Adenosylcobalamin and cob(II)alamin as prosthetic groups of 2-methyleneglutarate mutase from Clostridium barkeri."
Michel C., Albracht S.P., Buckel W.
Eur. J. Biochem. 205:767-773(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR.
[6]"On the role of two different cobalt(II) species in coenzyme B12-dependent 2-methyleneglutarate mutase from Clostridium barkeri."
Zelder O., Buckel W.
Biol. Chem. Hoppe-Seyler 374:85-90(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR.
[7]"Searching for intermediates in the carbon skeleton rearrangement of 2-methyleneglutarate to (R)-3-methylitaconate catalyzed by coenzyme B12-dependent 2-methyleneglutarate mutase from Eubacterium barkeri."
Pierik A.J., Ciceri D., Lopez R.F., Kroll F., Broker G., Beatrix B., Buckel W., Golding B.T.
Biochemistry 44:10541-10551(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, MUTAGENESIS OF HIS-464; ASP-483 AND HIS-485.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X77484 Genomic DNA. Translation: CAA54625.1.
DQ310789 Genomic DNA. Translation: ABC88403.1.
PIRS43237.

3D structure databases

ProteinModelPortalQ59268.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11712.
UniPathwayUPA01010; UER01016.

Family and domain databases

Gene3D3.40.50.280. 1 hit.
InterProIPR006159. Acid_CoA_mut_C.
IPR016176. Cbl-dep_enz_cat.
IPR006158. Cobalamin-bd.
[Graphical view]
PfamPF02310. B12-binding. 1 hit.
[Graphical view]
SUPFAMSSF51703. SSF51703. 1 hit.
SSF52242. SSF52242. 1 hit.
TIGRFAMsTIGR00640. acid_CoA_mut_C. 1 hit.
PROSITEPS51332. B12_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMGM_EUBBA
AccessionPrimary (citable) accession number: Q59268
Secondary accession number(s): Q0QLE7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: November 1, 1996
Last modified: October 16, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways