NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.00810-06; PubMed=16980466 [NCBI, ExPASy, EBI, Israel, Japan]
Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
"The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.";
J. Bacteriol. 188:7922-7931(2006).

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 (By similarity).
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 (By similarity).
SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein (Potential).
SIMILARITY: Belongs to the mtrF 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

AJ132817; CAB41643.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000099; AAZ70220.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_304800.1; -.

3D structure databases

ModBase

Q9Y8K5.

Enzyme and pathway databases

BioCyc

MBAR269797:MBAR_A1257-MON; -.

Ontologies

GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from HAMAP).
GO:0030269;	Molecular function: tetrahydromethanopterin S-methyltransferase activity (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01099; -; 1.
PBIL [Tree]

InterPro

IPR011307; MeTrfase_F.
IPR013347; MeTrfase_F_su.
Graphical view of domain structure.

PIRSF

PIRSF006523; MtrF; 1.

TIGR02507; MtrF; 1.

Genome annotation databases

GeneID

3627857; -.

GenomeReviews

CP000099_GR; Mbar_A1257.

KEGG

mba:Mbar_A1257; -.

NMPDR

fig|269797.3.peg.1263; -.

Phylogenomic databases

HOGENOM

Q9Y8K5; -.

Genome annotation databases

CMR

Q9Y8K5; Mbar_A1257.

Other

UniRef

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

Keywords

Cell membrane; Complete proteome; Membrane; Methanogenesis; Methyltransferase; One-carbon metabolism; Transferase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 73`	`73`	`Tetrahydromethanopterin S-methyltransferase subunit F.`	`PRO_0000147547`
`TRANSMEM`	`52 72`	`21`	`Potential.`

Sequence information

Length: 73 AA [This is the length of the unprocessed precursor]

Molecular weight: 7978 Da [This is the MW of the unprocessed precursor]

CRC64: C74C43B6B0310038 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKVAEEYDKG VPMMLAPQMG AIDATVESIR YRAQLIARNQ KLDSGVAATG MIGFAAGFLF 

        70 
SLLMVIVLPL LFW

Q9Y8K5 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