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; Multi-pass membrane protein (Potential).
SIMILARITY: Belongs to the mtrE 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; CAB41638.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000099; AAZ70225.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_304805.1; -.

3D structure databases

ModBase

Q9Y8K0.

Enzyme and pathway databases

BioCyc

MBAR269797:MBAR_A1262-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from HAMAP).
GO:0012506;	Cellular component: vesicle membrane (inferred from electronic annotation from InterPro).
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).
GO:0006814;	Biological process: sodium ion transport (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_01098; -; 1.
PBIL [Tree]

InterPro

IPR005780; MeTrfase_E.
Graphical view of domain structure.

Pfam

PF04206; MtrE; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF016509; MtrE; 1.

TIGRFAMs

TIGR01113; mtrE; 1.

ProtoNet

Q9Y8K0.

Genome annotation databases

GeneID

3627862; -.

GenomeReviews

CP000099_GR; Mbar_A1262.

KEGG

mba:Mbar_A1262; -.

NMPDR

fig|269797.3.peg.1268; -.

Phylogenomic databases

HOGENOM

Q9Y8K0; -.

Genome annotation databases

CMR

Q9Y8K0; Mbar_A1262.

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`	`1 302`	`302`	`Tetrahydromethanopterin S-methyltransferase subunit E.`	`PRO_0000147537`
`TRANSMEM`	`3 23`	`21`	`Potential.`
`TRANSMEM`	`86 106`	`21`	`Potential.`
`TRANSMEM`	`132 152`	`21`	`Potential.`
`TRANSMEM`	`155 175`	`21`	`Potential.`
`TRANSMEM`	`233 253`	`21`	`Potential.`
`TRANSMEM`	`259 279`	`21`	`Potential.`

Sequence information

Length: 302 AA [This is the length of the unprocessed precursor]

Molecular weight: 32507 Da [This is the MW of the unprocessed precursor]

CRC64: 78BE4AE4E0A9A182 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEPLISMGVL ALIGVAATIA GASEDLESDI GSQSNPNSQV QLAPQMMFPH RIFNKAISGE 

        70         80         90        100        110        120 
PPSNALMCSI GAAVATVLIS EFTMSPLFAL VFGSLIAACV HATFAVTSTM GRCASQSRFK 

       130        140        150        160        170        180 
QPIYLDMIRS HITPIMGYAF ITTFCILVVS YLMTVVLGHP FPLTMLAFIW GITIGAIGSS 

       190        200        210        220        230        240 
TGDVHYGAER EFQQFEFGSG LNASNSGNIV RYAESGLRDG FDNSWFCAKF GGPVTGLAFG 

       250        260        270        280        290        300 
MTVFLGSWIT TIFDPAKGLG WLSVIAGIVI VFILIIWNWK MEVYARKAYG PYKEDKTEEA 


SA

Q9Y8K0 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