Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q49173 (MCRZ_METFV) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 73. 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 gamma

Short name=MCR II gamma
EC=2.8.4.1
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase gamma
Gene names
Name:mrtG
Synonyms:mcrIIG
Ordered Locus Names:Mfer_0733
OrganismMethanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S) [Complete proteome] [HAMAP]
Taxonomic identifier523846 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanothermaceaeMethanothermus

Protein attributes

Sequence length267 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.

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 – 267267Methyl-coenzyme M reductase II subunit gamma
PRO_0000147475

Sequences

Sequence LengthMass (Da)Tools
Q49173 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 150D5FFAE6BC6F9D

FASTA26730,847
        10         20         30         40         50         60 
MAYEPQFNPG ETKIAENRRK HMNPNYELKK LREIADEDIV RVLGHRSPGE SFKTVHPPLE 

        70         80         90        100        110        120 
EMDFEEDPMK DIVEPIEGAK QGTRIRYIQF ADSMYNAPAQ PYDRARTYMW RFRGVDTGTL 

       130        140        150        160        170        180 
SGRQVIEMRE LDLEKVSKIL LETEIFDPAR CGIRGATVHG HSLRFDENGL MFDALQRYIY 

       190        200        210        220        230        240 
DEDSGHVVYV KDQVGRPLDQ PVDMGEPLPE DELKEITTIY RKDNIGMRED EELLEVVNKI 

       250        260 
HEARTIGGFG MEVFKKDLNK RLGGANE 

« 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70765 Genomic DNA. Translation: CAA50043.1.
CP002278 Genomic DNA. Translation: ADP77532.1.
PIRS43900.
RefSeqYP_004004294.1. NC_014658.1.

3D structure databases

ProteinModelPortalQ49173.
SMRQ49173. Positions 6-251.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADP77532; ADP77532; Mfer_0733.
GeneID9962463.
KEGGmfv:Mfer_0733.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000225820.
KOK00402.
OMAGHRNPGE.

Enzyme and pathway databases

BioCycMFER523846:GC24-762-MONOMER.
UniPathwayUPA00646; UER00699.

Family and domain databases

Gene3D3.90.320.20. 1 hit.
InterProIPR009024. Me_CoM_Rdtase_Fd-like_fold.
IPR003178. Me_CoM_Rdtase_gsu.
[Graphical view]
PfamPF02240. MCR_gamma. 1 hit.
[Graphical view]
PIRSFPIRSF000264. Meth_CoM_rd_gama. 1 hit.
ProDomPD005845. Me_CoM_Rdtase_gsu. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF55088. SSF55088. 1 hit.
TIGRFAMsTIGR03259. met_CoM_red_gam. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMCRZ_METFV
AccessionPrimary (citable) accession number: Q49173
Secondary accession number(s): E3GZ00
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: November 1, 1996
Last modified: October 16, 2013
This is version 73 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