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Reviewed, UniProtKB/Swiss-Prot Q49606 (MTRE_METKA)

Last modified June 16, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tetrahydromethanopterin S-methyltransferase subunit E
    EC=2.1.1.86
Alternative name(s):
    N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit E
Gene names
Name: mtrE
Ordered Locus Names: MK0656
OrganismMethanopyrus kandleri [Complete proteome] [HAMAP]
Taxonomic identifier2320 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (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. HAMAP MF_01098

Pathway

One-carbon metabolism; methanogenesis from carbone dioxide; methyl-CoM from 5,10-methylene-H(4)MPT: step 2/2. HAMAP MF_01098

Subunit structure

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.

Sequence similarities

Belongs to the mtrE family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 298298Tetrahydromethanopterin S-methyltransferase subunit E HAMAP MF_01098
PRO_0000147540

Regions

Transmembrane3 – 2321 Potential
Transmembrane59 – 7921 Potential
Transmembrane84 – 10421 Potential
Transmembrane132 – 15221 Potential
Transmembrane160 – 18021 Potential
Transmembrane230 – 25021 Potential
Transmembrane251 – 27121 Potential

Sequences

Sequence LengthMass (Da)Tools
Q49606-1 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: B540A568D1168C4C

FASTA29831,527
        10         20         30         40         50         60 
MVGFTEIGLA AAMGALATIA GAFEDAESDV GSQSNPNSQV QLAPQMMNFH RYFNKAISGE 

        70         80         90        100        110        120 
PVSYMLYGAI AGTVTWVMMT KFGLPFLAAA AVGVGVNALI HMVFATTAHL GRMASAAEFG 

       130        140        150        160        170        180 
HPIYLDVVLS HLGPIAGFGG IATFAIVSLA YIQWALLKHP FPLPLLAALW GVTVGAIGSS 

       190        200        210        220        230        240 
TGDVHYGAER LYQHYPFGGG VPVAAHGNIT RKAETGIRNS MDSVYFCAKF GNPLTGLCFG 

       250        260        270        280        290 
LVVFFSTWAG LFGQWGAVIA MGLVTLGCLI VSNRVEKKAR ESYGTYEDVE MDEICDPV 

« Hide

References

« Hide 'large scale' references
[1]"Identification of the active site histidine in the corrinoid protein MtrA of the energy-conserving methyltransferase complex from Methanobacterium thermoautotrophicum."
Harms U., Thauer R.K.
Eur. J. Biochem. 250:783-788(1997) [PubMed: 9461302] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens."
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed: 11930014] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.
[3]"Phylogeny of Methanopyrus kandleri based on methyl coenzyme M reductase operons."
Noelling J., Elfner A., Palmer J.R., Steigerwald V.J., Pihl T.D., Lake J.A., Reeve J.N.
Int. J. Syst. Bacteriol. 46:1170-1173(1996) [PubMed: 8863453] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89.

Cross-references

Sequence databases

Y14428 Genomic DNA. Translation: CAA74774.1.
AE010359 Genomic DNA. Translation: AAM01871.1.
U57340 Genomic DNA. Translation: AAB02004.1.
RefSeqNP_613941.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1476757.
GenomeReviewsGene locus MK0656 in contig AE009439_GR.
KEGGmka:MK0656.
NMPDRfig|190192.1.peg.654.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ49606.
OMAQ49606. SNPNSQV.

Enzyme and pathway databases

BioCycMKAN190192:MK0656-MON.
BRENDA2.1.1.86. 7577.

Family and domain databases

HAMAPMF_01098.
[Tree]
InterProIPR005780. MeTrfase_E.
[Graphical view]
PfamPF04206. MtrE. 1 hit.
[Graphical view]
PIRSFPIRSF016509. MtrE. 1 hit.
TIGRFAMsTIGR01113. mtrE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMTRE_METKA
AccessionPrimary (citable) accession number: Q49606
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1999
Last modified: June 16, 2009
This is version 56 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents