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P21111 (MCRY_METTH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 II subunit beta

Short name=MCR II beta
EC=2.8.4.1
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase beta
Gene names
Name:mrtB
Ordered Locus Names:MTH_1132
OrganismMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) [Reference proteome] [HAMAP]
Taxonomic identifier187420 [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 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.

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.

Sequence caution

The sequence AAB85621.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processMethanogenesis
   Molecular functionTransferase
   Technical termComplete proteome
Direct protein sequencing
Reference 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 Ref.4
Chain2 – 443442Methyl-coenzyme M reductase II subunit beta
PRO_0000147469

Experimental info

Sequence conflict2941Y → I in AAA73436. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P21111 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 462293DE946E994E

FASTA44347,134
        10         20         30         40         50         60 
MPMYEDRIDL YGADGKLLEE DVPLEAVSPL KNPTIANLVS DVKRSVAVNL AGIEGSLKKA 

        70         80         90        100        110        120 
ALGGKSNFIP GREVELPIVE NAEAIAEKVK RLVQTSEDDD TNIRLINNGQ QILVQVPTTR 

       130        140        150        160        170        180 
MGVAADYTVS ALVTGAAVVQ AIIDEFDVDM FDANAVKTAV MGRYPQTVDF TGANLSTLLG 

       190        200        210        220        230        240 
PPVLLEGLGY GLRNIMANHV VAITRKNTLN ASALSSILEQ TAMFETGDAV GAFERMHLLG 

       250        260        270        280        290        300 
LAYQGLNANN LLFDLVKENS KGTVGTVIAS LVERAIEDRV IKVASEMKSG YKMYEPADWA 

       310        320        330        340        350        360 
LWNAYAATGL LAATIVNVGA ARAAQGVAST VLYYNDILEY ETGLPGVDFG RAMGTAVGFS 

       370        380        390        400        410        420 
FFSHSIYGGG GPGIFHGNHV VTRHSKGFAL PCVAAAMCLD AGTQMFSVEK TSGLIGSVYS 

       430        440 
EIDYFREPIV NVAKGAAEIK DQL 

« Hide

References

« Hide 'large scale' references
[1]"Growth phase-dependent transcription of the genes that encode the two methyl coenzyme M reductase isoenzymes and N5-methyltetrahydromethanopterin:coenzyme M methyltransferase in Methanobacterium thermoautotrophicum delta H."
Pihl T.D., Sharma S., Reeve J.N.
J. Bacteriol. 176:6384-6391(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
[2]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
[3]"A hydrogenase-linked gene in Methanobacterium thermoautotrophicum strain delta H encodes a polyferredoxin."
Reeve J.N., Beckler G.S., Cram D.S., Hamilton P.T., Brown J.W., Krzycki J.A., Kolodziej A.F., Alex L., Orme-Johnson W.H., Walsh C.T.
Proc. Natl. Acad. Sci. U.S.A. 86:3031-3035(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-146.
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
[4]"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 2-20.
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09990 Genomic DNA. Translation: AAA73436.1.
AE000666 Genomic DNA. Translation: AAB85621.1. Different initiation.
J04540 Genomic DNA. Translation: AAB02353.1.
PIRG69017.
T45147.
RefSeqNP_276260.1. NC_000916.1.

3D structure databases

ProteinModelPortalP21111.
SMRP21111. Positions 4-443.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP21111. 1 interaction.
STRING187420.MTH1132.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB85621; AAB85621; MTH_1132.
GeneID1471540.
KEGGmth:MTH1132.

Phylogenomic databases

eggNOGCOG4054.
KOK00401.
OMAWALWNAY.

Enzyme and pathway databases

BioCycMetaCyc:MRTBMAUTO-MONOMER.
MTHE187420:GJNM-1134-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...

Entry information

Entry nameMCRY_METTH
AccessionPrimary (citable) accession number: P21111
Secondary accession number(s): O27204
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 101 of the entry and version 4 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