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Q49171 (MCRY_METFV) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 80. 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
Synonyms:mcrIIB
Ordered Locus Names:Mfer_0731
OrganismMethanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S) [Complete proteome] [HAMAP]
Taxonomic identifier523846 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanothermaceaeMethanothermus

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

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 By similarity.

Ontologies

Keywords
   Biological processMethanogenesis
   Molecular functionTransferase
   Technical termComplete 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

Chain1 – 443443Methyl-coenzyme M reductase II subunit beta
PRO_0000147464

Sequences

Sequence LengthMass (Da)Tools
Q49171 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: FEAA6DDD20A262E6

FASTA44347,447
        10         20         30         40         50         60 
MAIYEDKIDL YDANGKLLDE NVPLEAISPL KNPTIGKIVN DVKRSVAVNL AGIENSLKKA 

        70         80         90        100        110        120 
ALGGKANFIP GRELDLDIVE NAEIIAEKIK KMVQVDENDD TNVKMINNGQ QLLVQVPTIR 

       130        140        150        160        170        180 
IERAADYTVS TLVAGAATIQ AIIDTFDVDM FDASTVKTAV LGRYPQTVDF TGANVAAMLS 

       190        200        210        220        230        240 
PPVLLEGLGY GLRNILTNHI VATTKKNTLN AAALSSILEQ TAMFETGDAV GAFERLHLLG 

       250        260        270        280        290        300 
LAYQGLNADN LVYDLVKENK KGTVGTVIAS LVERAIEDKV IKVSKEMPSG FRVYEPIDWA 

       310        320        330        340        350        360 
LWNAYAAAGL LAATIVNIGA ARAAQGVAST VLYYNDILEY ETGLPGVDFG RAEGTAVGFS 

       370        380        390        400        410        420 
FFSHSIYGGG GPGIFHGNHV VTRHSKGFAL PCVAAAMSLD AGTQMFSPER TSGLVGQVYS 

       430        440 
EIDYFREPIK YVAEGAAKIK NKI 

« Hide

References

« Hide 'large scale' references
[1]"Characterization and phylogeny of mcrII, a gene cluster encoding an isoenzyme of methyl coenzyme M reductase from hyperthermophilic Methanothermus fervidus."
Lehmacher A., Klenk H.-P.
Mol. Gen. Genet. 243:198-206(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43054 / DSM 2088 / JCM 10308 / V24 S.
[2]"Complete genome sequence of Methanothermus fervidus type strain (V24S)."
Anderson I., Djao O.D., Misra M., Chertkov O., Nolan M., Lucas S., Lapidus A., Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N. expand/collapse author list , Pati A., Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Sikorski J., Spring S., Rohde M., Eichinger K., Huber H., Wirth R., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.
Stand. Genomic Sci. 3:315-324(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43054 / DSM 2088 / JCM 10308 / V24 S.
[3]Steigerwald V.J., Stroup D., Hennigan A.N., Pihl T.D., Reeve J.N.
Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70765 Genomic DNA. Translation: CAA50041.1.
CP002278 Genomic DNA. Translation: ADP77530.1.
M99219 Genomic DNA. Translation: AAA73384.1.
PIRS43899.
RefSeqYP_004004292.1. NC_014658.1.

3D structure databases

ProteinModelPortalQ49171.
SMRQ49171. Positions 2-443.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADP77530; ADP77530; Mfer_0731.
GeneID9962461.
KEGGmfv:Mfer_0731.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000225842.
KOK00401.
OMAWALWNAY.

Enzyme and pathway databases

BioCycMFER523846:GC24-760-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_METFV
AccessionPrimary (citable) accession number: Q49171
Secondary accession number(s): E3GYZ8, Q49177
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: November 1, 1996
Last modified: October 16, 2013
This is version 80 of the entry and version 1 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