O30640 (MTBA_METBA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methylcobamide:CoM methyltransferase MtbA
EC=2.1.1.247

Alternative name(s):
MT2-A
Methylcobamide:CoM methyltransferase II isozyme A
[Methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M

Gene names

Name:	mtbA
Synonyms:	cmtA

Organism

Methanosarcina barkeri

Taxonomic identifier

2208 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Methyltransferase involved in methanogenesis from methylamines methanol pathway. Catalyzes the transfer of the methyl group from the methylated corrinoid protein MtmC (MtmC1 or MtmC2) to coenzyme M, forming the substrate for coenzyme-B sulfoethylthiotransferase. Ref.1 Ref.3 Ref.7
Catalytic activity	A [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M = methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]. Ref.1 Ref.3 Ref.7
Cofactor	Zinc.
Enzyme regulation	Inhibited by EDTA and EGTA.
Pathway	One-carbon metabolism; methanogenesis from methylated amine.
Sequence similarities	Belongs to the uroporphyrinogen decarboxylase family. MtbA/MtaA subfamily.

Ontologies

Keywords
Biological process	Methanogenesis
Ligand	Metal-binding Zinc
Molecular function	Methyltransferase Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	methanogenesis Inferred from electronic annotation. Source: UniProtKB-KW one-carbon metabolic process Inferred from electronic annotation. Source: InterPro porphyrin-containing compound biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular_function	dimethylamine methyltransferase activity Inferred from direct assay Ref.7. Source: MENGO metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW uroporphyrinogen decarboxylase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 339	338	Methylcobamide:CoM methyltransferase MtbA		PRO_0000187667
Sites
	Metal binding	239	1	Zinc By similarity
	Metal binding	241	1	Zinc By similarity
	Metal binding	316	1	Zinc Potential
Natural variations
	Natural variant	226	1	V → A in strain: NIH.
	Natural variant	249	1	G → E in strain: NIH.

Sequences

	Sequence		Length	Mass (Da)
	O30640 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 63708390ED84FB12	FASTA	339	36,664
	10 20 30 40 50 60 MAEYTPKERL YRALRKQQVD RMPAVCFTQT ATVEQMEACG AYWPEAHSDA EKMATLAEAA 70 80 90 100 110 120 HTVVGFEAVR VPFDITAEAE FFGCGIKAGD LKQQPSVIKP SVKNLEDLEK LKNYNLKEGR 130 140 150 160 170 180 IAVVLEAVKI LSEKYGKELP IIGSMIGPFS LAQHINGDAW FGNLFTGEEV VPALLDFCSD 190 200 210 220 230 240 FNVAYAKAMV ENGADTIAII DPTASYELIG GEFYEKYALP YQKKIVDAMK ELDVATVLHI 250 260 270 280 290 300 CGNTTNGLGI MDKTGVNGIS VDQKVDIKTA TGSVKNAIIV GNLDPVAVLW NGTPEEIAEA 310 320 330 SKKALDAGVG LLTVGCGTVS MTPTVNLQKM IECAKSHTY

References

[1]	"Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri: physicochemical characterization, cloning, sequence analysis, and heterologous gene expression." Leclerc G.M., Grahame D.A. J. Biol. Chem. 271:18725-18731(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY. Strain: NIH.
[2]	"Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine." Burke S.A., Lo S.L., Krzycki J.A. J. Bacteriol. 180:3432-3440(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474.
[3]	"Involvement of the 'A' isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine." Burke S.A., Krzycki J.A. J. Bacteriol. 177:4410-4416(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-25, FUNCTION, CATALYTIC ACTIVITY. Strain: ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474.
[4]	"Specific roles of methylcobamide:coenzyme M methyltransferase isozymes in metabolism of methanol and methylamines in Methanosarcina barkeri." Ferguson D.J. Jr., Krzycki J.A., Grahame D.A. J. Biol. Chem. 271:5189-5194(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[5]	"Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri." Ferguson D.J. Jr., Krzycki J.A. J. Bacteriol. 179:846-852(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474.
[6]	"Reconstitution of monomethylamine:coenzyme M methyl transfer with a corrinoid protein and two methyltransferases purified from Methanosarcina barkeri." Burke S.A., Krzycki J.A. J. Biol. Chem. 272:16570-16577(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474.
[7]	"Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri." Ferguson D.J. Jr., Gorlatova N., Grahame D.A., Krzycki J.A. J. Biol. Chem. 275:29053-29060(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY. Strain: ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U38919 Genomic DNA. Translation: AAC44214.1. AF013713 Genomic DNA. Translation: AAC38632.1.
3D structure databases
ProteinModelPortal	O30640.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-12205.
UniPathway	UPA00650.
Family and domain databases
InterPro	IPR006360. Mtase_MtaA_CmuA. IPR000257. Uroporphyrinogen_deCOase. [Graphical view]
Pfam	PF01208. URO-D. 1 hit. [Graphical view]
TIGRFAMs	TIGR01463. mtaA_cmuA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MTBA_METBA

Accession

Primary (citable) accession number: O30640
Secondary accession number(s): Q48928

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 68 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program