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P07955 (MCRB_METBF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 106. 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 subunit beta

EC=2.8.4.1
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase beta
Gene names
Name:mcrB
Ordered Locus Names:Mbar_A0897
OrganismMethanosarcina barkeri (strain Fusaro / DSM 804) [Complete proteome] [HAMAP]
Taxonomic identifier269797 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length434 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 By similarity.

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.

Ontologies

Keywords
   Biological processMethanogenesis
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processmethanogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncoenzyme-B sulfoethylthiotransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 434433Methyl-coenzyme M reductase subunit beta
PRO_0000147462

Secondary structure

.......................................................................... 434
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07955 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A85044187FB78CB9

FASTA43445,421
        10         20         30         40         50         60 
MSDTVDIYDD RGKLLESNVD IMSLAPTRNA AIQSIIMDTK RSVAVNLAGI QGALASGKMG 

        70         80         90        100        110        120 
GKGRQILGRG LNYDIVGNAD AIAENVKKLV QVDEGDDTNV IKVKGGKSLL IQSPKSRIIA 

       130        140        150        160        170        180 
GADFMSATTV GAAAVTQTIM DMFGTDPYDA PIVKSAVWGS YPQTMDLMGG QVQGILSIPQ 

       190        200        210        220        230        240 
NNEGLGFSLR NIMANHVAAI SNRNAMNASA LSSIYEQSGI FEMGGAVGMF ERHQLLGLAY 

       250        260        270        280        290        300 
QGLNANNLLY DIVKENGKDG TIGTVIESVV RRAIEAGIIS VDKTAPSGYN FYKANDVPKW 

       310        320        330        340        350        360 
NACAAVGTLA ATLVNCGAGR AAQNVSSTLL YFNDILEKET GLPGCDYGKV EGTAVGFSFF 

       370        380        390        400        410        420 
SHSIYGGGGP GVFNGNHVVT RHSRGFAIPC VCAAVALDAG TQMFSIESTS GLIGDVFGAI 

       430 
PEFREPIKAV AGVL 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the methyl coenzyme M reductase gene cluster from Methanosarcina barkeri."
Bokranz M., Klein A.
Nucleic Acids Res. 15:4350-4351(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes."
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.
J. Bacteriol. 188:7922-7931(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Fusaro / DSM 804.
[3]"Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation."
Grabarse W., Mahlert F., Shima S., Thauer R.K., Ermler U.
J. Mol. Biol. 303:329-344(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00158 Genomic DNA. Translation: CAA68353.1.
CP000099 Genomic DNA. Translation: AAZ69871.1.
PIRA29525.
RefSeqYP_304451.1. NC_007355.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E6YX-ray1.60B/E2-434[»]
ProteinModelPortalP07955.
SMRP07955. Positions 2-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269797.Mbar_A0897.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ69871; AAZ69871; Mbar_A0897.
GeneID3625942.
KEGGmba:Mbar_A0897.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4054.
HOGENOMHOG000225842.
KOK00401.
OMAFREPLKY.

Enzyme and pathway databases

BioCycMBAR269797:GHUW-911-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

EvolutionaryTraceP07955.

Entry information

Entry nameMCRB_METBF
AccessionPrimary (citable) accession number: P07955
Secondary accession number(s): Q46E21
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 106 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