O30642 (MTMB1_METBA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Monomethylamine methyltransferase MtmB1
Short name=MMA methyltransferase 1
Short name=MMAMT 1
EC=2.1.1.248

Gene names

Name:	mtmB1
Synonyms:	mtmB

Organism

Methanosarcina barkeri

Taxonomic identifier

2208 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	458 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	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 process	Methanogenesis
Coding sequence diversity	Pyrrolysine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	methanogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	methyltransferase activity 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

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 458

457

Monomethylamine methyltransferase MtmB1

PRO_0000216550

Amino acid modifications

Non-standard residue

202

1

Pyrrolysine

Natural variations

Natural variant

36

1

A → S in strain: NIH.

Natural variant

219

1

T → A in strain: NIH.

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

458

Helix Strand Turn

Details...

Helix

9 – 18

10

Beta strand

19 – 21

3

Helix

24 – 28

5

Helix

31 – 42

12

Helix

56 – 73

18

Beta strand

75 – 77

3

Turn

78 – 81

4

Beta strand

82 – 84

3

Helix

88 – 95

8

Beta strand

101 – 105

5

Helix

107 – 109

3

Beta strand

111 – 114

4

Beta strand

125 – 129

5

Helix

137 – 139

3

Helix

140 – 148

9

Beta strand

155 – 157

3

Beta strand

160 – 162

3

Helix

174 – 193

20

Beta strand

201 – 203

3

Helix

210 – 214

5

Beta strand

226 – 231

6

Turn

234 – 236

3

Helix

240 – 251

12

Beta strand

255 – 259

5

Beta strand

266 – 268

3

Helix

271 – 288

18

Beta strand

292 – 296

5

Turn

301 – 303

3

Helix

309 – 325

17

Beta strand

330 – 333

4

Beta strand

340 – 342

3

Helix

343 – 359

17

Beta strand

362 – 366

5

Helix

370 – 372

3

Helix

380 – 393

14

Helix

398 – 410

13

Turn

411 – 414

4

Helix

425 – 428

4

Turn

431 – 434

4

Helix

438 – 453

16

Sequences

	Sequence		Length	Mass (Da)
	O30642 [UniParc]. Last modified February 26, 2008. Version 6. Checksum: CB75A20B1E5C0A2C	FASTA	458	50,238
	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

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), MASS SPECTROMETRY, PYRROLYSINE AT PYL-202.
+	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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L2Q	X-ray	1.70	A	1-458	[»]
1NTH	X-ray	1.55	A	1-458	[»]
1TV2	X-ray	2.00	A	1-458	[»]
1TV3	X-ray	2.20	A	1-458	[»]
1TV4	X-ray	1.80	A	1-458	[»]

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-12210.

UniPathway

UPA00643.

Family and domain databases

InterPro

IPR008031. MtmB_MeTrfase.
[Graphical view]

Pfam

PF05369. MtmB. 1 hit.
[Graphical view]

SUPFAM

SSF75098. MtmB_mtfrase. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

O30642.

Entry information

Entry name

MTMB1_METBA

Accession

Primary (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:	April 3, 2013
This is version 71 of the entry and version 6 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program