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O30642

- MTMB1_METBA

UniProt

O30642 - MTMB1_METBA

Protein

Monomethylamine methyltransferase MtmB1

Gene

mtmB1

Organism
Methanosarcina barkeri
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 6 (26 Feb 2008)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of the methyl group from monomethylamine to the corrinoid cofactor of MtmC (MtmC1 or MtmC2).2 Publications

    Catalytic activityi

    Methylamine + a [Co(I) methylamine-specific corrinoid protein] = a [methyl-Co(III) methylamine-specific corrinoid protein] + ammonia.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. monomethylamine methyltransferase activity Source: MENGO

    GO - Biological processi

    1. methanogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Methanogenesis

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-12210.
    UniPathwayiUPA00643.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Monomethylamine methyltransferase MtmB1 (EC:2.1.1.248)
    Short name:
    MMA methyltransferase 1
    Short name:
    MMAMT 1
    Gene namesi
    Name:mtmB1
    Synonyms:mtmB
    OrganismiMethanosarcina barkeri
    Taxonomic identifieri2208 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 458457Monomethylamine methyltransferase MtmB1PRO_0000216550Add
    BLAST

    Interactioni

    Subunit structurei

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

    Structurei

    Secondary structure

    1
    458
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 1810
    Beta strandi19 – 213
    Helixi24 – 285
    Helixi31 – 4212
    Helixi56 – 7318
    Beta strandi75 – 773
    Turni78 – 814
    Beta strandi82 – 843
    Helixi88 – 958
    Beta strandi101 – 1055
    Helixi107 – 1093
    Beta strandi111 – 1144
    Beta strandi125 – 1295
    Helixi137 – 1393
    Helixi140 – 1489
    Beta strandi155 – 1573
    Beta strandi160 – 1623
    Helixi174 – 19320
    Helixi209 – 2135
    Beta strandi225 – 2306
    Turni233 – 2353
    Helixi239 – 25012
    Beta strandi254 – 2585
    Beta strandi265 – 2673
    Helixi270 – 28718
    Beta strandi291 – 2955
    Turni300 – 3023
    Helixi308 – 32417
    Beta strandi329 – 3324
    Beta strandi339 – 3413
    Helixi342 – 35817
    Beta strandi361 – 3655
    Helixi369 – 3713
    Helixi379 – 39214
    Helixi397 – 40913
    Turni410 – 4134
    Helixi415 – 4173
    Helixi424 – 4274
    Turni430 – 4334
    Helixi437 – 45317

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1L2QX-ray1.70A1-457[»]
    1NTHX-ray1.55A1-457[»]
    1TV2X-ray2.00A1-457[»]
    1TV3X-ray2.20A1-457[»]
    1TV4X-ray1.80A1-457[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO30642.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.20.20.460. 1 hit.
    InterProiIPR008031. MtmB_MeTrfase.
    [Graphical view]
    PfamiPF05369. MtmB. 1 hit.
    [Graphical view]
    SUPFAMiSSF75098. SSF75098. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O30642-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTFRKSFDCY DFYDRAKVGE KCTQDDWDLM KIPMKAMELK QKYGLDFKGE    50
    FIPTDKDMME KLFKAGFEML LECGIYCTDT HRIVKYTEDE IWDAINNVQK 100
    EFVLGTGRDA VNVRKRSVGD KAKPIVQGGP TGSPISEDVF MPVHMSYALE 150
    KEVDTIVNGV MTSVRGKSPI PKSPYEVLAA KTETRLIKNA CAMAGRPGMG 200
    VOGPETSLSA QGNISADCTG GMTCTDSHEV SQLNELKIDL DAISVIAHYK 250
    GNSDIIMDEQ MPIFGGYAGG IEETTIVDVA THINAVLMSS ASWHLDGPVH 300
    IRWGSTNTRE TLMIAGWACA TISEFTDILS GNQYYPCAGP CTEMCLLEAS 350
    AQSITDTASG REILSGVASA KGVVTDKTTG MEARMMGEVA RATAGVEISE 400
    VNVILDKLVS LYEKNYASAP AGKTFQECYD VKTVTPTEEY MQVYDGARKK 450
    LEDLGLVF 458
    Length:458
    Mass (Da):50,238
    Last modified:February 26, 2008 - v6
    Checksum:iCB75A20B1E5C0A2C
    GO

    Mass spectrometryi

    Molecular mass is 50105±2 Da from positions 2 - 458. Determined by ESI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361A → S in strain: NIH.
    Natural varianti219 – 2191T → A in strain: NIH.

    Non-standard residue

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-standard residuei202 – 2021Pyrrolysine

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF013713 Genomic DNA. Translation: AAC38636.3.
    AF046875 Genomic DNA. Translation: AAC38637.1.

    Keywords - Coding sequence diversityi

    Pyrrolysine

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Life's jokers - Issue 25 of August 2002

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF013713 Genomic DNA. Translation: AAC38636.3 .
    AF046875 Genomic DNA. Translation: AAC38637.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1L2Q X-ray 1.70 A 1-457 [» ]
    1NTH X-ray 1.55 A 1-457 [» ]
    1TV2 X-ray 2.00 A 1-457 [» ]
    1TV3 X-ray 2.20 A 1-457 [» ]
    1TV4 X-ray 1.80 A 1-457 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00643 .
    BioCyci MetaCyc:MONOMER-12210.

    Miscellaneous databases

    EvolutionaryTracei O30642.

    Family and domain databases

    Gene3Di 3.20.20.460. 1 hit.
    InterProi IPR008031. MtmB_MeTrfase.
    [Graphical view ]
    Pfami PF05369. MtmB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF75098. SSF75098. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiMTMB1_METBA
    AccessioniPrimary (citable) accession number: O30642
    Secondary accession number(s): O52752
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2002
    Last sequence update: February 26, 2008
    Last modified: October 1, 2014
    This is version 79 of the entry and version 6 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    MtmB1 transcript is abundant relative to the mtmB2 transcript.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3