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Q59268

- MGM_EUBBA

UniProt

Q59268 - MGM_EUBBA

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Protein

2-methyleneglutarate mutase

Gene
mgm
Organism
Eubacterium barkeri (Clostridium barkeri)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

2-methyleneglutarate = 2-methylene-3-methylsuccinate.4 Publications

Cofactori

Cobalamin. Contains a mixture of adenosylcobalamin and oxygen-stable cob(II)alamin.5 Publications

Enzyme regulationi

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+.2 Publications

pH dependencei

Activity decreases rapidly below pH 7.5 in phosphate buffer, and below pH 8.0 in Tris buffer.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi485 – 4851Cobalt (cobalamin axial ligand) By similarity

GO - Molecular functioni

  1. 2-methyleneglutarate mutase activity Source: UniProtKB
  2. cobalamin binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cofactor catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Cobalamin, Cobalt, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11712.
UniPathwayiUPA01010; UER01016.

Names & Taxonomyi

Protein namesi
Recommended name:
2-methyleneglutarate mutase (EC:5.4.99.4)
Alternative name(s):
Alpha-methyleneglutarate mutase
Gene namesi
Name:mgm
OrganismiEubacterium barkeri (Clostridium barkeri)
Taxonomic identifieri1528 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesEubacteriaceaeEubacterium

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi464 – 4641H → Q: No effect on activity. 1 Publication
Mutagenesisi483 – 4831D → N: Activity reduced 2000-fold. 1 Publication
Mutagenesisi485 – 4851H → Q: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6146142-methyleneglutarate mutasePRO_0000096464Add
BLAST

Expressioni

Inductioni

By nicotinate.2 Publications

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ59268.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini472 – 614143B12-bindingAdd
BLAST

Sequence similaritiesi

Contains 1 B12-binding domain.

Family and domain databases

Gene3Di3.40.50.280. 1 hit.
InterProiIPR006159. Acid_CoA_mut_C.
IPR016176. Cbl-dep_enz_cat.
IPR006158. Cobalamin-bd.
[Graphical view]
PfamiPF02310. B12-binding. 1 hit.
[Graphical view]
SUPFAMiSSF51703. SSF51703. 1 hit.
SSF52242. SSF52242. 1 hit.
TIGRFAMsiTIGR00640. acid_CoA_mut_C. 1 hit.
PROSITEiPS51332. B12_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q59268-1 [UniParc]FASTAAdd to Basket

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MQEKTKRIIK EDIEAVRAYS DCFDVEMPDL DENGEVIGLP APYPREVAGT    50
VRSGYRIYDL AKKAKERGWP IQNPILGRNT AEETYGESQE MYAYADKFDE 100
TLFHFVHAEA TRHIDPLKGR ELINQSRGKG GITPIGEREF IAMGGGSKHP 150
VRINATGDTP HLSIINALIA GFDGTDIGPV IHVHFGGRGI HDYKTKVVNG 200
YKAIQICAEN NIFVQLDSHK HLNNIGGTDG MALAMCLLSE GLAVHAGLPW 250
ELSAIQMNVA GINIYADLAV MRAFRKACHS KSIIAVPETF QNPPGNLVAE 300
AAHFSRMAVT AKLGGADFYR PKAAESVGIP TGDSMGQAIW GTEDVFGHVV 350
NPDIQSPVID AREAEIIDEA LAVLEATLHL EGLTLEAMTD DFWKQWSDEA 400
LIDLIVAAGK AGVLDSQRAA GWDLKRHVVV NRDKDGITRY VKGYTPLGVD 450
ASRCAQSDED VEVHVEKAPT RPEKIVLATV GADAHVNGIN VIREAFQDAG 500
YDVVYLRGMN LPESVAEVAA EVGADAVGVS NLLGLGMELF PRVSKRLEEL 550
GLRDKMVVCA GGRIAEKEEE HRQFEEKIQK EGSAFMGMDG FFGPGSSPED 600
CVKIIGDMIN AKKA 614
Length:614
Mass (Da):66,750
Last modified:November 1, 1996 - v1
Checksum:i37B78FEB06A4A3D1
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971K → W AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X77484 Genomic DNA. Translation: CAA54625.1.
DQ310789 Genomic DNA. Translation: ABC88403.1.
PIRiS43237.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X77484 Genomic DNA. Translation: CAA54625.1 .
DQ310789 Genomic DNA. Translation: ABC88403.1 .
PIRi S43237.

3D structure databases

ProteinModelPortali Q59268.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA01010 ; UER01016 .
BioCyci MetaCyc:MONOMER-11712.

Family and domain databases

Gene3Di 3.40.50.280. 1 hit.
InterProi IPR006159. Acid_CoA_mut_C.
IPR016176. Cbl-dep_enz_cat.
IPR006158. Cobalamin-bd.
[Graphical view ]
Pfami PF02310. B12-binding. 1 hit.
[Graphical view ]
SUPFAMi SSF51703. SSF51703. 1 hit.
SSF52242. SSF52242. 1 hit.
TIGRFAMsi TIGR00640. acid_CoA_mut_C. 1 hit.
PROSITEi PS51332. B12_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiMGM_EUBBA
AccessioniPrimary (citable) accession number: Q59268
Secondary accession number(s): Q0QLE7
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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