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UniProtKB - Q59268 (MGM_EUBBA)
Protein
2-methyleneglutarate mutase
Gene
mgm
Organism
Eubacterium barkeri (Clostridium barkeri)
Status
Functioni
Involved in the fermentation of nicotinate to ammonia, propionate, acetate and carbon dioxide.
Catalytic activityi
- EC:5.4.99.44 Publications
Cofactori
adenosylcob(III)alamin5 Publications, cob(II)alamin5 PublicationsNote: Contains a mixture of adenosylcobalamin and oxygen-stable cob(II)alamin.5 Publications
Activity 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
: nicotinate degradation Pathwayi
This protein is involved in step 5 of the subpathway that synthesizes propanoate and pyruvate from 6-hydroxynicotinate.1 Publication 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 485 | Cobalt (adenosylcob(III)alamin axial ligand)By similarity | 1 |
GO - Molecular functioni
- 2-methyleneglutarate mutase activity Source: UniProtKB
- cobalamin binding Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- nicotinate catabolic process Source: UniProtKB
Keywordsi
Molecular function | Isomerase |
Ligand | Cobalamin, Cobalt, Metal-binding |
Enzyme and pathway databases
UniPathwayi | UPA01010;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 |
Organismi | Eubacterium barkeri (Clostridium barkeri) |
Taxonomic identifieri | 1528 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Clostridia › Eubacteriales › Eubacteriaceae › Eubacterium |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 464 | H → Q: No effect on activity. 1 Publication | 1 | |
Mutagenesisi | 483 | D → N: Activity reduced 2000-fold. 1 Publication | 1 | |
Mutagenesisi | 485 | H → Q: Loss of activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000096464 | 1 – 614 | 2-methyleneglutarate mutaseAdd BLAST | 614 |
Expressioni
Inductioni
By nicotinate.1 Publication
Interactioni
Subunit structurei
Homotetramer.
1 PublicationProtein-protein interaction databases
STRINGi | 1528.SAMN04488579_1129 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 472 – 614 | B12-bindingPROSITE-ProRule annotationAdd BLAST | 143 |
Family and domain databases
InterProi | View protein in InterPro IPR006159, Acid_CoA_mut_C IPR016176, Cbl-dep_enz_cat IPR006158, Cobalamin-bd IPR036724, Cobalamin-bd_sf |
Pfami | View protein in Pfam PF02310, B12-binding, 1 hit |
SUPFAMi | SSF51703, SSF51703, 1 hit SSF52242, SSF52242, 1 hit |
TIGRFAMsi | TIGR00640, acid_CoA_mut_C, 1 hit |
PROSITEi | View protein in PROSITE PS51332, B12_BINDING, 1 hit |
i Sequence
Sequence statusi: Complete.
Q59268-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 97 | K → W AA sequence (PubMed:8168499).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X77484 Genomic DNA Translation: CAA54625.1 DQ310789 Genomic DNA Translation: ABC88403.1 |
PIRi | S43237 |
Genome annotation databases
KEGGi | ag:CAA54625 |
Similar proteinsi
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 |
PIRi | S43237 |
3D structure databases
AlphaFoldDBi | Q59268 |
SMRi | Q59268 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 1528.SAMN04488579_1129 |
Genome annotation databases
KEGGi | ag:CAA54625 |
Enzyme and pathway databases
UniPathwayi | UPA01010;UER01016 |
Family and domain databases
InterProi | View protein in InterPro IPR006159, Acid_CoA_mut_C IPR016176, Cbl-dep_enz_cat IPR006158, Cobalamin-bd IPR036724, Cobalamin-bd_sf |
Pfami | View protein in Pfam PF02310, B12-binding, 1 hit |
SUPFAMi | SSF51703, SSF51703, 1 hit SSF52242, SSF52242, 1 hit |
TIGRFAMsi | TIGR00640, acid_CoA_mut_C, 1 hit |
PROSITEi | View protein in PROSITE PS51332, B12_BINDING, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | MGM_EUBBA | |
Accessioni | Q59268Primary (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: | May 25, 2022 | |
This is version 87 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencingDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways