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P11560 (MCRB_METTM) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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 beta

Short name=MCR I beta
EC=2.8.4.1
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase beta
Gene names
Name:mcrB
Ordered Locus Names:MTBMA_c15520
OrganismMethanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) [Complete proteome] [HAMAP]
Taxonomic identifier79929 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length443 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 a 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 direct assay Ref.1. Source: MENGO

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 443442Methyl-coenzyme M reductase I subunit beta
PRO_0000147468

Secondary structure

.................................................................................. 443
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11560 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1237E83E405E6D6B

FASTA44347,240
        10         20         30         40         50         60 
MAKFEDKVDL YDDRGNLVEE QVPLEALSPL RNPAIKSIVQ GIKRTVAVNL EGIENALKTA 

        70         80         90        100        110        120 
KVGGPACKIM GRELDLDIVG NAESIAAAAK EMIQVTEDDD TNVELLGGGK RALVQVPSAR 

       130        140        150        160        170        180 
FDVAAEYSAA PLVTATAFVQ AIINEFDVSM YDANMVKAAV LGRYPQSVEY MGANIATMLD 

       190        200        210        220        230        240 
IPQKLEGPGY ALRNIMVNHV VAATLKNTLQ AAALSTILEQ TAMFEMGDAV GAFERMHLLG 

       250        260        270        280        290        300 
LAYQGMNADN LVFDLVKANG KEGTVGSVIA DLVERALEDG VIKVEKELTD YKVYGTDDLA 

       310        320        330        340        350        360 
MWNAYAAAGL MAATMVNQGA ARAAQGVSST LLYYNDLIEF ETGLPSVDFG KVEGTAVGFS 

       370        380        390        400        410        420 
FFSHSIYGGG GPGIFNGNHI VTRHSKGFAI PCVAAAMALD AGTQMFSPEA TSGLIKEVFS 

       430        440 
QVDEFREPLK YVVEAAAEIK NEI 

« 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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: CAA30635.1.
CP001710 Genomic DNA. Translation: ADL59131.1.
PIRA28544.
RefSeqYP_003850444.1. NC_014408.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HBMX-ray1.80B/E2-443[»]
1HBNX-ray1.16B/E2-443[»]
1HBOX-ray1.78B/E2-443[»]
1HBUX-ray1.90B/E2-443[»]
1MROX-ray1.16B/E2-443[»]
3M1VX-ray1.45B/E2-443[»]
3M2RX-ray1.30B/E2-443[»]
3M2UX-ray1.40B/E2-443[»]
3M2VX-ray1.80B/E2-443[»]
3M30X-ray1.45B/E2-443[»]
3M32X-ray1.35B/E2-443[»]
3POTX-ray1.20B/E1-443[»]
ProteinModelPortalP11560.
SMRP11560. Positions 2-443.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADL59131; ADL59131; MTBMA_c15520.
GeneID9705261.
KEGGmmg:MTBMA_c15520.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000225842.
KOK00401.
OMAFREPLKY.
ProtClustDBCLSK876059.

Enzyme and pathway databases

BioCycMMAR79929:GH5J-1556-MONOMER.
UniPathwayUPA00646; UER00699.

Family and domain databases

Gene3D1.20.840.10. 2 hits.
3.30.70.470. 1 hit.
InterProIPR022681. MCR_a/b_chain_a-bundle.
IPR008924. Me_CoM_Rdtase_asu/bsu_C.
IPR015823. Me_CoM_Rdtase_asu_N_sub2.
IPR003179. Me_CoM_Rdtase_bsu.
IPR022679. Me_CoM_Rdtase_bsu_C.
IPR022680. Me_CoM_Rdtase_bsu_N.
IPR009024. Me_CoM_Rdtase_Fd-like_fold.
[Graphical view]
PfamPF02241. MCR_beta. 1 hit.
PF02783. MCR_beta_N. 1 hit.
[Graphical view]
PIRSFPIRSF000263. Meth_CoM_rd_beta. 1 hit.
SUPFAMSSF48081. SSF48081. 1 hit.
SSF55088. SSF55088. 1 hit.
TIGRFAMsTIGR03257. met_CoM_red_bet. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP11560.

Entry information

Entry nameMCRB_METTM
AccessionPrimary (citable) accession number: P11560
Secondary accession number(s): D9PY33
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways