Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Methyl-coenzyme M reductase subunit gamma

Gene

mcrG

Organism
Methanothermus fervidus
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
OrganismiMethanothermus fervidus
Taxonomic identifieri2180 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanothermaceaeMethanothermus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249Methyl-coenzyme M reductase subunit gammaPRO_0000147474Add
BLAST

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP12973.
SMRiP12973. Positions 2-247.
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.

P12973-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQFYPGSTK IAENRRKFMN PDAELEKLRE ISDEDVVRIL GHRAPGEEYP
60 70 80 90 100
SVHPPLEELD EPEDPIKDIV EPTEGAKAGD RVRYVQFTDS VYFAPAQPYI
110 120 130 140 150
RSRAYLWRYR GADAGTLSGR QIIEARERDV EKIAKELIET EFFDPARTGI
160 170 180 190 200
RGKSVHGHSL RLDENGMMFD MLRRQVYDEE TGRVKMVKNQ IGDEFDEPID
210 220 230 240
LGEPLDEETL KEKTTIYRID NIPYREDKDL LEIVQRIHQL RSEAGFSPE
Length:249
Mass (Da):28,856
Last modified:October 1, 1989 - v1
Checksum:i9EBC01D15018300F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03375 Genomic DNA. Translation: AAA72196.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03375 Genomic DNA. Translation: AAA72196.1.

3D structure databases

ProteinModelPortaliP12973.
SMRiP12973. Positions 2-247.
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. "Structure and comparative analysis of the genes encoding component C of methyl coenzyme M reductase in the extremely thermophilic archaebacterium Methanothermus fervidus."
    Weil C.F., Cram D.S., Sherf B.A., Reeve J.N.
    J. Bacteriol. 170:4718-4726(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiMCRG_METFE
AccessioniPrimary (citable) accession number: P12973
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: September 3, 2014
This is version 70 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.