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O30642 (MTMB1_METBA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Monomethylamine methyltransferase MtmB1

Short name=MMA methyltransferase 1
Short name=MMAMT 1
EC=2.1.1.248
Gene names
Name:mtmB1
Synonyms:mtmB
OrganismMethanosarcina barkeri
Taxonomic identifier2208 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of the methyl group from monomethylamine to the corrinoid cofactor of MtmC (MtmC1 or MtmC2). Ref.1 Ref.3

Catalytic activity

Methylamine + a [Co(I) methylamine-specific corrinoid protein] = a [methyl-Co(III) methylamine-specific corrinoid protein] + ammonia. Ref.3

Pathway

One-carbon metabolism; methanogenesis from methylamine.

Subunit structure

Dimer of homotrimers. Can form a complex with MtmC (MtmC1 or MtmC2).

Miscellaneous

MtmB1 transcript is abundant relative to the mtmB2 transcript.

Sequence similarities

Belongs to the monomethylamine methyltransferase family.

Mass spectrometry

Molecular mass is 50105±2 Da from positions 2 - 458. Determined by ESI. Ref.2

Ontologies

Keywords
   Biological processMethanogenesis
   Coding sequence diversityPyrrolysine
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processmethanogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmonomethylamine methyltransferase activity

Inferred from direct assay Ref.1. Source: MENGO

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 458457Monomethylamine methyltransferase MtmB1
PRO_0000216550

Amino acid modifications

Non-standard residue2021Pyrrolysine

Natural variations

Natural variant361A → S in strain: NIH.
Natural variant2191T → A in strain: NIH.

Secondary structure

........................................................................... 458
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O30642 [UniParc].

Last modified February 26, 2008. Version 6.
Checksum: CB75A20B1E5C0A2C

FASTA45850,238
        10         20         30         40         50         60 
MTFRKSFDCY DFYDRAKVGE KCTQDDWDLM KIPMKAMELK QKYGLDFKGE FIPTDKDMME 

        70         80         90        100        110        120 
KLFKAGFEML LECGIYCTDT HRIVKYTEDE IWDAINNVQK EFVLGTGRDA VNVRKRSVGD 

       130        140        150        160        170        180 
KAKPIVQGGP TGSPISEDVF MPVHMSYALE KEVDTIVNGV MTSVRGKSPI PKSPYEVLAA 

       190        200        210        220        230        240 
KTETRLIKNA CAMAGRPGMG VOGPETSLSA QGNISADCTG GMTCTDSHEV SQLNELKIDL 

       250        260        270        280        290        300 
DAISVIAHYK GNSDIIMDEQ MPIFGGYAGG IEETTIVDVA THINAVLMSS ASWHLDGPVH 

       310        320        330        340        350        360 
IRWGSTNTRE TLMIAGWACA TISEFTDILS GNQYYPCAGP CTEMCLLEAS AQSITDTASG 

       370        380        390        400        410        420 
REILSGVASA KGVVTDKTTG MEARMMGEVA RATAGVEISE VNVILDKLVS LYEKNYASAP 

       430        440        450 
AGKTFQECYD VKTVTPTEEY MQVYDGARKK LEDLGLVF 

« Hide

References

[1]"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], FUNCTION.
Strain: ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474 and NIH.
[2]"The amber codon in the gene encoding the monomethylamine methyltransferase isolated from Methanosarcina barkeri is translated as a sense codon."
James C.M., Ferguson T.K., Leykam J.F., Krzycki J.A.
J. Biol. Chem. 276:34252-34258(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-7; 22-28; 189-213; 251-255; 408-411 AND 453-458, MASS SPECTROMETRY.
Strain: ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474.
[3]"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: FUNCTION, CATALYTIC ACTIVITY.
Strain: ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474.
[4]"The residue mass of L-pyrrolysine in three distinct methylamine methyltransferases."
Soares J.A., Zhang L., Pitsch R.L., Kleinholz N.M., Jones R.B., Wolff J.J., Amster J., Green-Church K.B., Krzycki J.A.
J. Biol. Chem. 280:36962-36969(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PYRROLYSINE AT PYL-202.
Strain: ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474.
[5]"A new UAG-encoded residue in the structure of a methanogen methyltransferase."
Hao B., Gong W., Ferguson T.K., James C.M., Krzycki J.A., Chan M.K.
Science 296:1462-1466(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS), PYRROLYSINE AT PYL-202, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Life's jokers - Issue 25 of August 2002

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF013713 Genomic DNA. Translation: AAC38636.3.
AF046875 Genomic DNA. Translation: AAC38637.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1L2QX-ray1.70A1-457[»]
1NTHX-ray1.55A1-457[»]
1TV2X-ray2.00A1-457[»]
1TV3X-ray2.20A1-457[»]
1TV4X-ray1.80A1-457[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12210.
UniPathwayUPA00643.

Family and domain databases

Gene3D3.20.20.460. 1 hit.
InterProIPR008031. MtmB_MeTrfase.
[Graphical view]
PfamPF05369. MtmB. 1 hit.
[Graphical view]
SUPFAMSSF75098. SSF75098. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO30642.

Entry information

Entry nameMTMB1_METBA
AccessionPrimary (citable) accession number: O30642
Secondary accession number(s): O52752
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: February 26, 2008
Last modified: May 14, 2014
This is version 78 of the entry and version 6 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways