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Protein

2-methyleneglutarate mutase

Gene

mgm

Organism
Eubacterium barkeri (Clostridium barkeri)
Status
Reviewed-Annotation score: 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

adenosylcob(III)alamin5 Publications, cob(II)alamin5 PublicationsNote: 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.1 Publication

Interactioni

Subunit structurei

Homotetramer.1 Publication

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

        10         20         30         40         50
MQEKTKRIIK EDIEAVRAYS DCFDVEMPDL DENGEVIGLP APYPREVAGT
60 70 80 90 100
VRSGYRIYDL AKKAKERGWP IQNPILGRNT AEETYGESQE MYAYADKFDE
110 120 130 140 150
TLFHFVHAEA TRHIDPLKGR ELINQSRGKG GITPIGEREF IAMGGGSKHP
160 170 180 190 200
VRINATGDTP HLSIINALIA GFDGTDIGPV IHVHFGGRGI HDYKTKVVNG
210 220 230 240 250
YKAIQICAEN NIFVQLDSHK HLNNIGGTDG MALAMCLLSE GLAVHAGLPW
260 270 280 290 300
ELSAIQMNVA GINIYADLAV MRAFRKACHS KSIIAVPETF QNPPGNLVAE
310 320 330 340 350
AAHFSRMAVT AKLGGADFYR PKAAESVGIP TGDSMGQAIW GTEDVFGHVV
360 370 380 390 400
NPDIQSPVID AREAEIIDEA LAVLEATLHL EGLTLEAMTD DFWKQWSDEA
410 420 430 440 450
LIDLIVAAGK AGVLDSQRAA GWDLKRHVVV NRDKDGITRY VKGYTPLGVD
460 470 480 490 500
ASRCAQSDED VEVHVEKAPT RPEKIVLATV GADAHVNGIN VIREAFQDAG
510 520 530 540 550
YDVVYLRGMN LPESVAEVAA EVGADAVGVS NLLGLGMELF PRVSKRLEEL
560 570 580 590 600
GLRDKMVVCA GGRIAEKEEE HRQFEEKIQK EGSAFMGMDG FFGPGSSPED
610
CVKIIGDMIN AKKA
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:
EMBLi
GenBanki
DDBJi
Links Updated
X77484 Genomic DNA. Translation: CAA54625.1.
DQ310789 Genomic DNA. Translation: ABC88403.1.
PIRiS43237.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77484 Genomic DNA. Translation: CAA54625.1.
DQ310789 Genomic DNA. Translation: ABC88403.1.
PIRiS43237.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA01010; UER01016.
BioCyciMetaCyc:MONOMER-11712.

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]
ProtoNetiSearch...

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: April 1, 2015
This is version 67 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

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 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.