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Protein

Methyl-coenzyme M reductase subunit gamma

Gene

mcrG

Organism
Methanococcus voltae
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein predictedi

Functioni

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

Catalytic activityi

Methyl-CoM + CoB = CoM-S-S-CoB + methane.

Pathwayi

GO - Molecular functioni

  1. coenzyme-B sulfoethylthiotransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. methanogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Methanogenesis

Enzyme and pathway databases

UniPathwayiUPA00646; UER00699.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-coenzyme M reductase subunit gamma (EC:2.8.4.1)
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase gamma
Gene namesi
Name:mcrG
OrganismiMethanococcus voltae
Taxonomic identifieri2188 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Methyl-coenzyme M reductase subunit gammaPRO_0000147484Add
BLAST

Interactioni

Subunit structurei

Hexamer of two alpha, two beta, and two gamma chains.

Structurei

3D structure databases

ProteinModelPortaliP11563.
SMRiP11563. Positions 6-250.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

Gene3Di3.90.320.20. 1 hit.
InterProiIPR009024. Me_CoM_Rdtase_Fd-like_fold.
IPR003178. Me_CoM_Rdtase_gsu.
[Graphical view]
PfamiPF02240. MCR_gamma. 1 hit.
[Graphical view]
PIRSFiPIRSF000264. Meth_CoM_rd_gama. 1 hit.
ProDomiPD005845. Me_CoM_Rdtase_gsu. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF55088. SSF55088. 1 hit.
TIGRFAMsiTIGR03259. met_CoM_red_gam. 1 hit.

Sequencei

Sequence statusi: Complete.

P11563-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYKPQFYPS ATKVAENRRN HINPAFELEK LREIPDEDVV KIMGHRQPSE
60 70 80 90 100
DYKTVHPPLE EMDLAEDYVR DLVGPINGAK EGHRIRYIQF ADSMYFAPSQ
110 120 130 140 150
PYDRSRLYMS RFRGVDCGTL SGRQVVELRE SNLEDISKNY LVDTELFDPA
160 170 180 190 200
TTGMRGATVH GHSLRLDENG VMFDALQRYE FDEATGHILY VKDQVGRPWD
210 220 230 240 250
EPVDVGEPVP QEKLKEITTI YRKDGVAMRD DMEVVEVVKR IHRARTLGGY
260
CPLNEIFDTY L
Length:261
Mass (Da):30,132
Last modified:October 1, 1989 - v1
Checksum:i236BA6C71F5AAA49
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07793 Genomic DNA. Translation: CAA30632.1.
PIRiS03260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07793 Genomic DNA. Translation: CAA30632.1.
PIRiS03260.

3D structure databases

ProteinModelPortaliP11563.
SMRiP11563. Positions 6-250.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00646; UER00699.

Family and domain databases

Gene3Di3.90.320.20. 1 hit.
InterProiIPR009024. Me_CoM_Rdtase_Fd-like_fold.
IPR003178. Me_CoM_Rdtase_gsu.
[Graphical view]
PfamiPF02240. MCR_gamma. 1 hit.
[Graphical view]
PIRSFiPIRSF000264. Meth_CoM_rd_gama. 1 hit.
ProDomiPD005845. Me_CoM_Rdtase_gsu. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF55088. SSF55088. 1 hit.
TIGRFAMsiTIGR03259. met_CoM_red_gam. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Comparative analysis of genes encoding methyl coenzyme M reductase in methanogenic bacteria."
    Klein A., Allmansberger R., Bokranz M., Knaub S., Mueller B., Muth E.
    Mol. Gen. Genet. 213:409-420(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS.

Entry informationi

Entry nameiMCRG_METVO
AccessioniPrimary (citable) accession number: P11563
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: September 3, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.