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P11562

- MCRG_METTM

UniProt

P11562 - MCRG_METTM

Protein

Methyl-coenzyme M reductase I subunit gamma

Gene

mcrG

Organism
Methanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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: MENGO

    GO - Biological processi

    1. methanogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Methanogenesis

    Enzyme and pathway databases

    BioCyciMMAR79929:GH5J-1553-MONOMER.
    UniPathwayiUPA00646; UER00699.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methyl-coenzyme M reductase I subunit gamma (EC:2.8.4.1)
    Short name:
    MCR I gamma
    Alternative name(s):
    Coenzyme-B sulfoethylthiotransferase gamma
    Gene namesi
    Name:mcrG
    Ordered Locus Names:MTBMA_c15490
    OrganismiMethanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
    Taxonomic identifieri79929 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
    ProteomesiUP000000345: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 249248Methyl-coenzyme M reductase I subunit gammaPRO_0000147479Add
    BLAST

    Expressioni

    Developmental stagei

    There are two MCR complexes in this bacteria. MCR II is expressed in the early growth phase. Late growth cells contains mostly MCR I.

    Interactioni

    Subunit structurei

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

    Structurei

    Secondary structure

    1
    249
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 1910
    Helixi33 – 408
    Beta strandi51 – 533
    Helixi56 – 583
    Helixi65 – 695
    Helixi74 – 785
    Beta strandi82 – 898
    Turni91 – 933
    Helixi98 – 10811
    Beta strandi113 – 1164
    Beta strandi121 – 1266
    Helixi127 – 13913
    Turni145 – 1473
    Beta strandi148 – 1503
    Beta strandi175 – 1773
    Turni179 – 1813
    Beta strandi184 – 1885
    Beta strandi194 – 2007
    Helixi207 – 2137
    Helixi224 – 2263
    Helixi228 – 24619

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HBMX-ray1.80C/F2-249[»]
    1HBNX-ray1.16C/F2-249[»]
    1HBOX-ray1.78C/F2-249[»]
    1HBUX-ray1.90C/F2-249[»]
    1MROX-ray1.16C/F2-248[»]
    3M1VX-ray1.45C/F2-249[»]
    3M2RX-ray1.30C/F2-249[»]
    3M2UX-ray1.40C/F2-249[»]
    3M2VX-ray1.80C/F2-249[»]
    3M30X-ray1.45C/F2-249[»]
    3M32X-ray1.35C/F2-249[»]
    3POTX-ray1.20C/F1-249[»]
    ProteinModelPortaliP11562.
    SMRiP11562. Positions 2-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11562.

    Family & Domainsi

    Phylogenomic databases

    HOGENOMiHOG000225820.
    KOiK00402.
    OMAiKRTTIYR.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P11562-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQYYPGTTK VAQNRRNFCN PEYELEKLRE ISDEDVVKIL GHRAPGEEYP    50
    SVHPPLEEMD EPEDAIREMV EPIDGAKAGD RVRYIQFTDS MYFAPAQPYV 100
    RSRAYLCRYR GADAGTLSGR QIIETRERDL EKISKELLET EFFDPARSGV 150
    RGKSVHGHSL RLDEDGMMFD MLRRQIYNKD TGRVEMVKNQ IGDELDEPVD 200
    LGEPLDEETL MEKTTIYRVD GEAYRDDVEA VEIMQRIHVL RSQGGFNLE 249
    Length:249
    Mass (Da):28,758
    Last modified:January 23, 2007 - v3
    Checksum:iE39CD62AD7CCC6DC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07794 Genomic DNA. Translation: CAA30638.1.
    CP001710 Genomic DNA. Translation: ADL59128.1.
    RefSeqiYP_003850441.1. NC_014408.1.

    Genome annotation databases

    EnsemblBacteriaiADL59128; ADL59128; MTBMA_c15490.
    GeneIDi9705258.
    KEGGimmg:MTBMA_c15490.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07794 Genomic DNA. Translation: CAA30638.1 .
    CP001710 Genomic DNA. Translation: ADL59128.1 .
    RefSeqi YP_003850441.1. NC_014408.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HBM X-ray 1.80 C/F 2-249 [» ]
    1HBN X-ray 1.16 C/F 2-249 [» ]
    1HBO X-ray 1.78 C/F 2-249 [» ]
    1HBU X-ray 1.90 C/F 2-249 [» ]
    1MRO X-ray 1.16 C/F 2-248 [» ]
    3M1V X-ray 1.45 C/F 2-249 [» ]
    3M2R X-ray 1.30 C/F 2-249 [» ]
    3M2U X-ray 1.40 C/F 2-249 [» ]
    3M2V X-ray 1.80 C/F 2-249 [» ]
    3M30 X-ray 1.45 C/F 2-249 [» ]
    3M32 X-ray 1.35 C/F 2-249 [» ]
    3POT X-ray 1.20 C/F 1-249 [» ]
    ProteinModelPortali P11562.
    SMRi P11562. Positions 2-248.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADL59128 ; ADL59128 ; MTBMA_c15490 .
    GeneIDi 9705258.
    KEGGi mmg:MTBMA_c15490.

    Phylogenomic databases

    HOGENOMi HOG000225820.
    KOi K00402.
    OMAi KRTTIYR.

    Enzyme and pathway databases

    UniPathwayi UPA00646 ; UER00699 .
    BioCyci MMAR79929:GH5J-1553-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P11562.

    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. "Cloning and characterization of the methyl coenzyme M reductase genes from Methanobacterium thermoautotrophicum."
      Bokranz M., Baeumner G., Allmansberger R., Ankel-Fuchs D., Klein A.
      J. Bacteriol. 170:568-577(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
    2. "Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism."
      Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., Gottschalk G., Thauer R.K.
      J. Bacteriol. 192:5850-5851(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
    3. "Two genetically distinct methyl-coenzyme M reductases in Methanobacterium thermoautotrophicum strain Marburg and delta H."
      Rospert S., Linder D., Ellermann J., Thauer R.K.
      Eur. J. Biochem. 194:871-877(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21.
      Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
    4. "Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation."
      Ermler U., Grabarse W., Shima S., Goubeaud M., Thauer R.K.
      Science 278:1457-1462(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
      Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
    5. "On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding."
      Grabarse W., Mahlert F., Duin E.C., Goubeaud M., Shima S., Thauer R.K., Lamzin V., Ermler U.
      J. Mol. Biol. 309:315-330(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS).
      Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.

    Entry informationi

    Entry nameiMCRG_METTM
    AccessioniPrimary (citable) accession number: P11562
    Secondary accession number(s): D9PY30
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 100 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3