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P11562 (MCRG_METTM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methyl-coenzyme M reductase I subunit gamma
Short name=MCR I gamma
EC=2.8.4.1
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase gamma
Gene names
Name:mcrG
Ordered Locus Names:MTBMA_c15490
OrganismMethanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) [Complete proteome] [HAMAP]
Taxonomic identifier79929 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and an heterodisulfide.

Catalytic activity

Methyl-CoM + CoB = CoM-S-S-CoB + methane.

Cofactor

Binds 2 coenzyme F430 noncovalently per hexamer. Coenzyme F430 is a yellow nickel porphinoid.

Pathway

One-carbon metabolism; methyl-coenzyme M reduction; methane from methyl-coenzyme M: step 1/1.

Subunit structure

Hexamer of two alpha, two beta, and two gamma chains.

Developmental stage

There are two MCR complexes in this bacteria. MCR II is expressed in the early growth phase. Late growth cells contains mostly MCR I.

Ontologies

Keywords
   Biological processMethanogenesis
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processmethanogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncoenzyme-B sulfoethylthiotransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 249248Methyl-coenzyme M reductase I subunit gamma
PRO_0000147479

Secondary structure

1 ......................................... 249
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11562 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E39CD62AD7CCC6DC

FASTA24928,758
        10         20         30         40         50         60 
MAQYYPGTTK VAQNRRNFCN PEYELEKLRE ISDEDVVKIL GHRAPGEEYP SVHPPLEEMD 

        70         80         90        100        110        120 
EPEDAIREMV EPIDGAKAGD RVRYIQFTDS MYFAPAQPYV RSRAYLCRYR GADAGTLSGR 

       130        140        150        160        170        180 
QIIETRERDL EKISKELLET EFFDPARSGV RGKSVHGHSL RLDEDGMMFD MLRRQIYNKD 

       190        200        210        220        230        240 
TGRVEMVKNQ IGDELDEPVD LGEPLDEETL MEKTTIYRVD GEAYRDDVEA VEIMQRIHVL 


RSQGGFNLE

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the methyl coenzyme M reductase genes from Methanobacterium thermoautotrophicum."
Bokranz M., Baeumner G., Allmansberger R., Ankel-Fuchs D., Klein A.
J. Bacteriol. 170:568-577(1988) [PubMed: 2448287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
[2]"Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism."
Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., Gottschalk G., Thauer R.K.
J. Bacteriol. 192:5850-5851(2010) [PubMed: 20802048] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
[3]"Two genetically distinct methyl-coenzyme M reductases in Methanobacterium thermoautotrophicum strain Marburg and delta H."
Rospert S., Linder D., Ellermann J., Thauer R.K.
Eur. J. Biochem. 194:871-877(1990) [PubMed: 2269306] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21.
Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
[4]"Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation."
Ermler U., Grabarse W., Shima S., Goubeaud M., Thauer R.K.
Science 278:1457-1462(1997) [PubMed: 9367957] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
[5]"On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding."
Grabarse W., Mahlert F., Duin E.C., Goubeaud M., Shima S., Thauer R.K., Lamzin V., Ermler U.
J. Mol. Biol. 309:315-330(2001) [PubMed: 11491299] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS).
Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X07794 Genomic DNA. Translation: CAA30638.1.
CP001710 Genomic DNA. Translation: ADL59128.1.
RefSeqYP_003850441.1. NC_014408.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HBMX-ray1.80C/F2-249[»]
1HBNX-ray1.16C/F2-249[»]
1HBOX-ray1.78C/F2-249[»]
1HBUX-ray1.90C/F2-249[»]
1MROX-ray1.16C/F2-248[»]
3M1VX-ray1.45C/F2-249[»]
3M2RX-ray1.30C/F2-249[»]
3M2UX-ray1.40C/F2-249[»]
3M2VX-ray1.80C/F2-249[»]
3M30X-ray1.45C/F2-249[»]
3M32X-ray1.35C/F2-249[»]
3POTX-ray1.20C/F1-249[»]
ProteinModelPortalP11562.
SMRP11562. Positions 2-248.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID9705258.
GenomeReviewsGene locus MTBMA_c15490 in contig CP001710_GR.
KEGGmmg:MTBMA_c15490.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAGHRAPGE.
ProtClustDBCLSK876060.

Family and domain databases

InterProIPR009024. Me_CoM_Rdtase_Fd-like_fold.
IPR003178. Me_CoM_Rdtase_gsu.
[Graphical view]
Gene3DG3DSA:3.90.320.20. MCR_gamma. 1 hit.
KOK00402.
PfamPF02240. MCR_gamma. 1 hit.
[Graphical view]
PIRSFPIRSF000264. Meth_CoM_rd_gama. 1 hit.
ProDomPD005845. Me_CoM_Rdtase_gsu. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF55088. MCR_fer_like. 1 hit.
TIGRFAMsTIGR03259. Met_CoM_red_gam. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMCRG_METTM
AccessionPrimary (citable) accession number: P11562
Secondary accession number(s): D9PY30
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents