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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: nicotinate degradation

This protein is involved in step 5 of the subpathway that synthesizes propanoate and pyruvate from 6-hydroxynicotinate.1 Publication
Proteins known to be involved in the 8 steps of the subpathway in this organism are:
  1. 6-hydroxynicotinate reductase (Hnr)
  2. Enamidase (Ena)
  3. 2-(hydroxymethyl)glutarate dehydrogenase (Hgd)
  4. no protein annotated in this organism
  5. 2-methyleneglutarate mutase (mgm)
  6. 3-methylitaconate isomerase (mii)
  7. 2,3-dimethylmalate dehydratase small subunit (DmdB), 2,3-dimethylmalate dehydratase large subunit (dmdA)
  8. 2,3-dimethylmalate lyase (Dml)
This subpathway is part of the pathway nicotinate degradation, which is itself part of Cofactor degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes propanoate and pyruvate from 6-hydroxynicotinate, the pathway nicotinate degradation and in Cofactor degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi485Cobalt (cobalamin axial ligand)By similarity1

GO - Molecular functioni

  • 2-methyleneglutarate mutase activity Source: UniProtKB
  • cobalamin binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi464H → Q: No effect on activity. 1 Publication1
Mutagenesisi483D → N: Activity reduced 2000-fold. 1 Publication1
Mutagenesisi485H → Q: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000964641 – 6142-methyleneglutarate mutaseAdd BLAST614

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)DescriptionActionsGraphical viewLength
Domaini472 – 614B12-bindingPROSITE-ProRule annotationAdd BLAST143

Sequence similaritiesi

Contains 1 B12-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

KOiK20450.

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)DescriptionActionsGraphical viewLength
Sequence conflicti97K → W AA sequence (PubMed:8168499).Curated1

Sequence databases

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

Genome annotation databases

KEGGiag:CAA54625.

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

ProteinModelPortaliQ59268.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA54625.

Phylogenomic databases

KOiK20450.

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...

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 5, 2016
This is version 70 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

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.