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Reviewed, UniProtKB/Swiss-Prot P11560 (MCRB_METTM)

Last modified September 22, 2009. Version 68. 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

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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
OrganismMethanobacterium thermoautotrophicum (strain Marburg / DSM 2133)
Taxonomic identifier79929 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

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Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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

Catalytic activity

2-(methylthio)ethanesulfonate (methyl-CoM) + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) = 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.

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Ontologies

Keywords
   Biological processMethanogenesis
   Molecular functionTransferase
   Technical term3D-structure
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 443442Methyl-coenzyme M reductase I subunit beta
PRO_0000147468

Secondary structure

1 .................................................................................. 443
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P11560-1 [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

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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].
[2]"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.
[3]"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).
[4]"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).

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Cross-references

Sequence databases

X07794 Genomic DNA. Translation: CAA30635.1.
PIRA28544.

3D structure databases

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[»]
ModBaseSearch...

Family and domain databases

InterProIPR008924. Me_CoM_Rdtase_asu/bsu_C.
IPR003179. Me_CoM_Rdtase_bsu.
[Graphical view]
Gene3DG3DSA:1.20.840.10. MCR_a/b_chain_a-bundle. 2 hits.
PfamPF02241. MCR_beta. 1 hit.
PF02783. MCR_beta_N. 1 hit.
[Graphical view]
PIRSFPIRSF000263. Meth_CoM_rd_beta. 1 hit.
TIGRFAMsTIGR03257. met_CoM_red_bet. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameMCRB_METTM
AccessionPrimary (citable) accession number: P11560
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: September 22, 2009
This is version 68 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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