[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND SUBUNIT. PubMed=7737157 [NCBI, ExPASy, EBI, Israel, Japan] Harms U., Weiss D.S., Gaertner P., Linder D., Thauer R.K.; "The energy conserving N5-methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum is composed of eight different subunits."; Eur. J. Biochem. 228:640-648(1995).
[2]	PROTEIN SEQUENCE OF 1-30. PubMed=8477726 [NCBI, ExPASy, EBI, Israel, Japan] Gaertner P., Ecker A., Fischer R., Linder D., Fuchs G., Thauer R.K.; "Purification and properties of N5-methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanobacterium thermoautotrophicum."; Eur. J. Biochem. 213:537-545(1993).
[3]	FUNCTION. DOI=10.1016/S0014-5793(99)00429-9; PubMed=10338124 [NCBI, ExPASy, EBI, Israel, Japan] Hippler B., Thauer R.K.; "The energy conserving methyltetrahydromethanopterin:coenzyme M methyltransferase complex from methanogenic archaea: function of the subunit MtrH."; FEBS Lett. 449:165-168(1999).

Comments

FUNCTION: Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step. MtrH catalyzes the transfer of the methyl group from methyl-tetrahydromethanopterin to the corrinoid prosthetic group of mtrA.
CATALYTIC ACTIVITY: 5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate = 5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate.
PATHWAY: One-carbon metabolism; methanogenesis from carbone dioxide; methyl-CoM from 5,10-methylene-H(4)MPT: step 2/2 .
SUBUNIT: The complex is composed of 8 subunits; mtrA, mtrB, mtrC, mtrD, mtrE, mtrF, mtrG and mtrH.
SIMILARITY: Belongs to the mtrH family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X84219; CAA59003.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

P80187.

Ontologies

GO:0030269;	Molecular function: tetrahydromethanopterin S-methyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0015948;	Biological process: methanogenesis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01501; -; 1.
PBIL [Tree]

InterPro

IPR002856; MtrH_MeTrfase.
Graphical view of domain structure.

Pfam

PF02007; MtrH; 1.
Pfam graphical view of domain structure.

ProDom

PD009948; MtrH_mtfrase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGR01114; mtrH; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Methanogenesis; Methyltransferase; One-carbon metabolism; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 310`	`310`		`Tetrahydromethanopterin S-methyltransferase subunit H.`	`PRO_0000147568`

Sequence information

Length: 310 AA [This is the length of the unprocessed precursor]

Molecular weight: 33474 Da [This is the MW of the unprocessed precursor]

CRC64: EB3B44FDD73F2A66 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFRFDKEQIV LDIAGTKIGG QPGEYPTVLA GTIFYGGHSI IEDEKAGVFD KDKAEALIKT 

        70         80         90        100        110        120 
QEEMSDVTGN PHIVQTFGQT PEAIVKYLEF VGDITDAPFF IDSTSGEARI AGAEYASEVG 

       130        140        150        160        170        180 
LEDRAIYNSV NMAADESELE ALKNTKLSAS IVLGFNPMDP TVEGKIGIWE DGAGTIDKGL 

       190        200        210        220        230        240 
LEMAADCGID KYLMDVAVTP LGQGAGVAVR TSFAVKSKWG YPVGSGIHNV PSAWDWLREY 

       250        260        270        280        290        300 
KKEHKEAWPV CDVGSNLIQQ MAGGDFVLYG PIENARMAFP ACAMADIFIS EAAKDIGTEA 

       310 
VEDHPFFKLL

P80187 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools