Q59268 (MGM_EUBBA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2-methyleneglutarate mutase
EC=5.4.99.4

Alternative name(s):
Alpha-methyleneglutarate mutase

Gene names

Name:

mgm

Organism

Eubacterium barkeri (Clostridium barkeri)

Taxonomic identifier

1528 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Eubacteriaceae › Eubacterium

Protein attributes

Sequence length	614 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the fermentation of nicotinate to ammonia, propionate, acetate and carbon dioxide.
Catalytic activity	2-methyleneglutarate = 2-methylene-3-methylsuccinate. Ref.1 Ref.3 Ref.4 Ref.7
Cofactor	Cobalamin. Contains a mixture of adenosylcobalamin and oxygen-stable cob(II)alamin. Ref.1 Ref.3 Ref.5 Ref.6 Ref.7
Enzyme regulation	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+. Ref.3 Ref.7
Pathway	Cofactor degradation; nicotinate degradation; propanoate and pyruvate from 6-hydroxynicotinate: step 5/8. Ref.2
Subunit structure	Homotetramer. Ref.4
Induction	By nicotinate. Ref.3 Ref.7
Sequence similarities	Contains 1 B12-binding domain.
Biophysicochemical properties	pH dependence: Activity decreases rapidly below pH 7.5 in phosphate buffer, and below pH 8.0 in Tris buffer. Ref.3

Ontologies

Keywords
Ligand	Cobalamin Cobalt Metal-binding
Molecular function	Isomerase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	cofactor catabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	2-methyleneglutarate mutase activity Inferred from direct assay Ref.1. Source: UniProtKB cobalamin binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 614	614	2-methyleneglutarate mutase		PRO_0000096464
Regions
	Domain	472 – 614	143	B12-binding
Sites
	Metal binding	485	1	Cobalt (cobalamin axial ligand) By similarity
Experimental info
	Mutagenesis	464	1	H → Q: No effect on activity. Ref.7
	Mutagenesis	483	1	D → N: Activity reduced 2000-fold. Ref.7
	Mutagenesis	485	1	H → Q: Loss of activity. Ref.7
	Sequence conflict	97	1	K → W AA sequence Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q59268 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 37B78FEB06A4A3D1	FASTA	614	66,750
	10 20 30 40 50 60 MQEKTKRIIK EDIEAVRAYS DCFDVEMPDL DENGEVIGLP APYPREVAGT VRSGYRIYDL 70 80 90 100 110 120 AKKAKERGWP IQNPILGRNT AEETYGESQE MYAYADKFDE TLFHFVHAEA TRHIDPLKGR 130 140 150 160 170 180 ELINQSRGKG GITPIGEREF IAMGGGSKHP VRINATGDTP HLSIINALIA GFDGTDIGPV 190 200 210 220 230 240 IHVHFGGRGI HDYKTKVVNG YKAIQICAEN NIFVQLDSHK HLNNIGGTDG MALAMCLLSE 250 260 270 280 290 300 GLAVHAGLPW ELSAIQMNVA GINIYADLAV MRAFRKACHS KSIIAVPETF QNPPGNLVAE 310 320 330 340 350 360 AAHFSRMAVT AKLGGADFYR PKAAESVGIP TGDSMGQAIW GTEDVFGHVV NPDIQSPVID 370 380 390 400 410 420 AREAEIIDEA LAVLEATLHL EGLTLEAMTD DFWKQWSDEA LIDLIVAAGK AGVLDSQRAA 430 440 450 460 470 480 GWDLKRHVVV NRDKDGITRY VKGYTPLGVD ASRCAQSDED VEVHVEKAPT RPEKIVLATV 490 500 510 520 530 540 GADAHVNGIN VIREAFQDAG YDVVYLRGMN LPESVAEVAA EVGADAVGVS NLLGLGMELF 550 560 570 580 590 600 PRVSKRLEEL GLRDKMVVCA GGRIAEKEEE HRQFEEKIQK EGSAFMGMDG FFGPGSSPED 610 CVKIIGDMIN AKKA

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X77484 Genomic DNA. Translation: CAA54625.1. DQ310789 Genomic DNA. Translation: ABC88403.1.
PIR	S43237.
3D structure databases
ProteinModelPortal	Q59268.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-11712.
UniPathway	UPA01010; UER01016.
Family and domain databases
Gene3D	3.40.50.280. 1 hit.
InterPro	IPR006159. Acid_CoA_mut_C. IPR006158. Cobalamin-bd. [Graphical view]
Pfam	PF02310. B12-binding. 1 hit. [Graphical view]
SUPFAM	SSF52242. Cbl-bd. 1 hit.
TIGRFAMs	TIGR00640. acid_CoA_mut_C. 1 hit.
PROSITE	PS51332. B12_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MGM_EUBBA

Accession

Primary (citable) accession number: Q59268
Secondary accession number(s): Q0QLE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2002
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program