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P12973

- MCRG_METFE

UniProt

P12973 - MCRG_METFE

Protein

Methyl-coenzyme M reductase subunit gamma

Gene

mcrG

Organism
Methanothermus fervidus
Status
Reviewed - Annotation score: 3 out of 5- Protein predictedi
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    • History
      Entry version 70 (03 Sep 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
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    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

    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

    MAQFYPGSTK IAENRRKFMN PDAELEKLRE ISDEDVVRIL GHRAPGEEYP    50
    SVHPPLEELD EPEDPIKDIV EPTEGAKAGD RVRYVQFTDS VYFAPAQPYI 100
    RSRAYLWRYR GADAGTLSGR QIIEARERDV EKIAKELIET EFFDPARTGI 150
    RGKSVHGHSL RLDENGMMFD MLRRQVYDEE TGRVKMVKNQ IGDEFDEPID 200
    LGEPLDEETL KEKTTIYRID NIPYREDKDL LEIVQRIHQL RSEAGFSPE 249
    Length:249
    Mass (Da):28,856
    Last modified:October 1, 1989 - v1
    Checksum:i9EBC01D15018300F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03375 Genomic DNA. Translation: AAA72196.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03375 Genomic DNA. Translation: AAA72196.1 .

    3D structure databases

    ProteinModelPortali P12973.
    SMRi P12973. Positions 2-247.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00646 ; UER00699 .

    Family and domain databases

    Gene3Di 3.90.320.20. 1 hit.
    InterProi IPR009024. Me_CoM_Rdtase_Fd-like_fold.
    IPR003178. Me_CoM_Rdtase_gsu.
    [Graphical view ]
    Pfami PF02240. MCR_gamma. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000264. Meth_CoM_rd_gama. 1 hit.
    ProDomi PD005845. Me_CoM_Rdtase_gsu. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF55088. SSF55088. 1 hit.
    TIGRFAMsi TIGR03259. met_CoM_red_gam. 1 hit.
    ProtoNeti Search...

    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