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O30642

- MTMB1_METBA

UniProt

O30642 - MTMB1_METBA

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Protein

Monomethylamine methyltransferase MtmB1

Gene

mtmB1

Organism
Methanosarcina barkeri
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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 – 1810Combined sources
Beta strandi19 – 213Combined sources
Helixi24 – 285Combined sources
Helixi31 – 4212Combined sources
Helixi56 – 7318Combined sources
Beta strandi75 – 773Combined sources
Turni78 – 814Combined sources
Beta strandi82 – 843Combined sources
Helixi88 – 958Combined sources
Beta strandi101 – 1055Combined sources
Helixi107 – 1093Combined sources
Beta strandi111 – 1144Combined sources
Beta strandi125 – 1295Combined sources
Helixi137 – 1393Combined sources
Helixi140 – 1489Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi160 – 1623Combined sources
Helixi174 – 19320Combined sources
Helixi210 – 2145Combined sources
Beta strandi226 – 2316Combined sources
Turni234 – 2363Combined sources
Helixi240 – 25112Combined sources
Beta strandi255 – 2595Combined sources
Beta strandi266 – 2683Combined sources
Helixi271 – 28818Combined sources
Beta strandi292 – 2965Combined sources
Turni301 – 3033Combined sources
Helixi309 – 32517Combined sources
Beta strandi330 – 3334Combined sources
Beta strandi340 – 3423Combined sources
Helixi343 – 35917Combined sources
Beta strandi362 – 3665Combined sources
Helixi370 – 3723Combined sources
Helixi380 – 39314Combined sources
Helixi398 – 41013Combined sources
Turni411 – 4144Combined sources
Helixi415 – 4173Combined sources
Helixi425 – 4284Combined sources
Turni431 – 4344Combined sources
Helixi438 – 45417Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L2QX-ray1.70A1-458[»]
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

        10         20         30         40         50
MTFRKSFDCY DFYDRAKVGE KCTQDDWDLM KIPMKAMELK QKYGLDFKGE
60 70 80 90 100
FIPTDKDMME KLFKAGFEML LECGIYCTDT HRIVKYTEDE IWDAINNVQK
110 120 130 140 150
EFVLGTGRDA VNVRKRSVGD KAKPIVQGGP TGSPISEDVF MPVHMSYALE
160 170 180 190 200
KEVDTIVNGV MTSVRGKSPI PKSPYEVLAA KTETRLIKNA CAMAGRPGMG
210 220 230 240 250
VOGPETSLSA QGNISADCTG GMTCTDSHEV SQLNELKIDL DAISVIAHYK
260 270 280 290 300
GNSDIIMDEQ MPIFGGYAGG IEETTIVDVA THINAVLMSS ASWHLDGPVH
310 320 330 340 350
IRWGSTNTRE TLMIAGWACA TISEFTDILS GNQYYPCAGP CTEMCLLEAS
360 370 380 390 400
AQSITDTASG REILSGVASA KGVVTDKTTG MEARMMGEVA RATAGVEISE
410 420 430 440 450
VNVILDKLVS LYEKNYASAP AGKTFQECYD VKTVTPTEEY MQVYDGARKK

LEDLGLVF
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AF013713 Genomic DNA. Translation: AAC38636.3 .
AF046875 Genomic DNA. Translation: AAC38637.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1L2Q X-ray 1.70 A 1-458 [» ]
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: November 26, 2014
This is version 81 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