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Q59268

- MGM_EUBBA

UniProt

Q59268 - MGM_EUBBA

Protein

2-methyleneglutarate mutase

Gene

mgm

Organism
Eubacterium barkeri (Clostridium barkeri)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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

    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.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ59268.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini472 – 614143B12-bindingPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 B12-binding domain.PROSITE-ProRule annotation

    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

    « Hide

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti97 – 971K → W AA sequence (PubMed:8168499)Curated

    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 1, 2014
    This is version 65 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