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P07955

- MCRB_METBF

UniProt

P07955 - MCRB_METBF

Protein

Methyl-coenzyme M reductase subunit beta

Gene

mcrB

Organism
Methanosarcina barkeri (strain Fusaro / DSM 804)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (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: UniProtKB-EC

    GO - Biological processi

    1. methanogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Methanogenesis

    Enzyme and pathway databases

    BioCyciMBAR269797:GHUW-911-MONOMER.
    UniPathwayiUPA00646; UER00699.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methyl-coenzyme M reductase subunit beta (EC:2.8.4.1)
    Alternative name(s):
    Coenzyme-B sulfoethylthiotransferase beta
    Gene namesi
    Name:mcrB
    Ordered Locus Names:Mbar_A0897
    OrganismiMethanosarcina barkeri (strain Fusaro / DSM 804)
    Taxonomic identifieri269797 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
    ProteomesiUP000008156: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 434433Methyl-coenzyme M reductase subunit betaPRO_0000147462Add
    BLAST

    Interactioni

    Subunit structurei

    Hexamer of two alpha, two beta, and two gamma chains.1 Publication

    Protein-protein interaction databases

    STRINGi269797.Mbar_A0897.

    Structurei

    Secondary structure

    1
    434
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Beta strandi14 – 207
    Helixi21 – 244
    Turni26 – 283
    Helixi30 – 4112
    Beta strandi42 – 465
    Helixi47 – 5610
    Helixi76 – 783
    Helixi79 – 9012
    Beta strandi99 – 1035
    Turni104 – 1074
    Beta strandi108 – 1125
    Helixi115 – 1195
    Beta strandi121 – 1244
    Helixi126 – 14217
    Helixi147 – 1493
    Helixi150 – 1589
    Turni159 – 1635
    Beta strandi164 – 1663
    Beta strandi171 – 1733
    Helixi179 – 1813
    Helixi188 – 1903
    Helixi194 – 2007
    Turni201 – 2033
    Helixi205 – 22218
    Helixi229 – 24315
    Helixi248 – 2569
    Turni257 – 2593
    Helixi262 – 27514
    Beta strandi278 – 2847
    Beta strandi290 – 2967
    Helixi297 – 31923
    Helixi322 – 3243
    Helixi325 – 34016
    Helixi345 – 3484
    Helixi349 – 35911
    Beta strandi362 – 3665
    Helixi370 – 3723
    Turni378 – 3803
    Beta strandi382 – 3876
    Helixi388 – 39710
    Helixi406 – 41712
    Helixi421 – 4244
    Helixi426 – 4316

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E6YX-ray1.60B/E2-434[»]
    ProteinModelPortaliP07955.
    SMRiP07955. Positions 2-434.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07955.

    Family & Domainsi

    Phylogenomic databases

    eggNOGiCOG4054.
    HOGENOMiHOG000225842.
    KOiK00401.
    OMAiFREPLKY.

    Family and domain databases

    Gene3Di1.20.840.10. 2 hits.
    3.30.70.470. 1 hit.
    InterProiIPR022681. MCR_a/b_chain_a-bundle.
    IPR008924. Me_CoM_Rdtase_asu/bsu_C.
    IPR015823. Me_CoM_Rdtase_asu_N_sub2.
    IPR003179. Me_CoM_Rdtase_bsu.
    IPR022679. Me_CoM_Rdtase_bsu_C.
    IPR022680. Me_CoM_Rdtase_bsu_N.
    IPR009024. Me_CoM_Rdtase_Fd-like_fold.
    [Graphical view]
    PfamiPF02241. MCR_beta. 1 hit.
    PF02783. MCR_beta_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000263. Meth_CoM_rd_beta. 1 hit.
    SUPFAMiSSF48081. SSF48081. 1 hit.
    SSF55088. SSF55088. 1 hit.
    TIGRFAMsiTIGR03257. met_CoM_red_bet. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P07955-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDTVDIYDD RGKLLESNVD IMSLAPTRNA AIQSIIMDTK RSVAVNLAGI    50
    QGALASGKMG GKGRQILGRG LNYDIVGNAD AIAENVKKLV QVDEGDDTNV 100
    IKVKGGKSLL IQSPKSRIIA GADFMSATTV GAAAVTQTIM DMFGTDPYDA 150
    PIVKSAVWGS YPQTMDLMGG QVQGILSIPQ NNEGLGFSLR NIMANHVAAI 200
    SNRNAMNASA LSSIYEQSGI FEMGGAVGMF ERHQLLGLAY QGLNANNLLY 250
    DIVKENGKDG TIGTVIESVV RRAIEAGIIS VDKTAPSGYN FYKANDVPKW 300
    NACAAVGTLA ATLVNCGAGR AAQNVSSTLL YFNDILEKET GLPGCDYGKV 350
    EGTAVGFSFF SHSIYGGGGP GVFNGNHVVT RHSRGFAIPC VCAAVALDAG 400
    TQMFSIESTS GLIGDVFGAI PEFREPIKAV AGVL 434
    Length:434
    Mass (Da):45,421
    Last modified:January 23, 2007 - v3
    Checksum:iA85044187FB78CB9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00158 Genomic DNA. Translation: CAA68353.1.
    CP000099 Genomic DNA. Translation: AAZ69871.1.
    PIRiA29525.
    RefSeqiWP_011305920.1. NC_007355.1.
    YP_304451.1. NC_007355.1.

    Genome annotation databases

    EnsemblBacteriaiAAZ69871; AAZ69871; Mbar_A0897.
    GeneIDi3625942.
    KEGGimba:Mbar_A0897.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00158 Genomic DNA. Translation: CAA68353.1 .
    CP000099 Genomic DNA. Translation: AAZ69871.1 .
    PIRi A29525.
    RefSeqi WP_011305920.1. NC_007355.1.
    YP_304451.1. NC_007355.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E6Y X-ray 1.60 B/E 2-434 [» ]
    ProteinModelPortali P07955.
    SMRi P07955. Positions 2-434.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 269797.Mbar_A0897.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAZ69871 ; AAZ69871 ; Mbar_A0897 .
    GeneIDi 3625942.
    KEGGi mba:Mbar_A0897.

    Phylogenomic databases

    eggNOGi COG4054.
    HOGENOMi HOG000225842.
    KOi K00401.
    OMAi FREPLKY.

    Enzyme and pathway databases

    UniPathwayi UPA00646 ; UER00699 .
    BioCyci MBAR269797:GHUW-911-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P07955.

    Family and domain databases

    Gene3Di 1.20.840.10. 2 hits.
    3.30.70.470. 1 hit.
    InterProi IPR022681. MCR_a/b_chain_a-bundle.
    IPR008924. Me_CoM_Rdtase_asu/bsu_C.
    IPR015823. Me_CoM_Rdtase_asu_N_sub2.
    IPR003179. Me_CoM_Rdtase_bsu.
    IPR022679. Me_CoM_Rdtase_bsu_C.
    IPR022680. Me_CoM_Rdtase_bsu_N.
    IPR009024. Me_CoM_Rdtase_Fd-like_fold.
    [Graphical view ]
    Pfami PF02241. MCR_beta. 1 hit.
    PF02783. MCR_beta_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000263. Meth_CoM_rd_beta. 1 hit.
    SUPFAMi SSF48081. SSF48081. 1 hit.
    SSF55088. SSF55088. 1 hit.
    TIGRFAMsi TIGR03257. met_CoM_red_bet. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the methyl coenzyme M reductase gene cluster from Methanosarcina barkeri."
      Bokranz M., Klein A.
      Nucleic Acids Res. 15:4350-4351(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes."
      Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.
      J. Bacteriol. 188:7922-7931(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Fusaro / DSM 804.
    3. "Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation."
      Grabarse W., Mahlert F., Shima S., Thauer R.K., Ermler U.
      J. Mol. Biol. 303:329-344(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiMCRB_METBF
    AccessioniPrimary (citable) accession number: P07955
    Secondary accession number(s): Q46E21
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 108 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, Reference proteome

    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