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P21111

- MCRY_METTH

UniProt

P21111 - MCRY_METTH

Protein

Methyl-coenzyme M reductase II subunit beta

Gene

mrtB

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 4 (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

    BioCyciMetaCyc:MRTBMAUTO-MONOMER.
    MTHE187420:GJNM-1134-MONOMER.
    UniPathwayiUPA00646; UER00699.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methyl-coenzyme M reductase II subunit beta (EC:2.8.4.1)
    Short name:
    MCR II beta
    Alternative name(s):
    Coenzyme-B sulfoethylthiotransferase beta
    Gene namesi
    Name:mrtB
    Ordered Locus Names:MTH_1132
    OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
    Taxonomic identifieri187420 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
    ProteomesiUP000005223: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 443442Methyl-coenzyme M reductase II subunit betaPRO_0000147469Add
    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.

    Protein-protein interaction databases

    IntActiP21111. 1 interaction.
    STRINGi187420.MTH1132.

    Structurei

    3D structure databases

    ProteinModelPortaliP21111.
    SMRiP21111. Positions 4-443.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Phylogenomic databases

    eggNOGiCOG4054.
    KOiK00401.
    OMAiWALWNAY.

    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.

    P21111-1 [UniParc]FASTAAdd to Basket

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    MPMYEDRIDL YGADGKLLEE DVPLEAVSPL KNPTIANLVS DVKRSVAVNL    50
    AGIEGSLKKA ALGGKSNFIP GREVELPIVE NAEAIAEKVK RLVQTSEDDD 100
    TNIRLINNGQ QILVQVPTTR MGVAADYTVS ALVTGAAVVQ AIIDEFDVDM 150
    FDANAVKTAV MGRYPQTVDF TGANLSTLLG PPVLLEGLGY GLRNIMANHV 200
    VAITRKNTLN ASALSSILEQ TAMFETGDAV GAFERMHLLG LAYQGLNANN 250
    LLFDLVKENS KGTVGTVIAS LVERAIEDRV IKVASEMKSG YKMYEPADWA 300
    LWNAYAATGL LAATIVNVGA ARAAQGVAST VLYYNDILEY ETGLPGVDFG 350
    RAMGTAVGFS FFSHSIYGGG GPGIFHGNHV VTRHSKGFAL PCVAAAMCLD 400
    AGTQMFSVEK TSGLIGSVYS EIDYFREPIV NVAKGAAEIK DQL 443
    Length:443
    Mass (Da):47,134
    Last modified:January 23, 2007 - v4
    Checksum:i462293DE946E994E
    GO

    Sequence cautioni

    The sequence AAB85621.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti294 – 2941Y → I in AAA73436. (PubMed:7929010)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09990 Genomic DNA. Translation: AAA73436.1.
    AE000666 Genomic DNA. Translation: AAB85621.1. Different initiation.
    J04540 Genomic DNA. Translation: AAB02353.1.
    PIRiG69017.
    T45147.
    RefSeqiNP_276260.1. NC_000916.1.

    Genome annotation databases

    EnsemblBacteriaiAAB85621; AAB85621; MTH_1132.
    GeneIDi1471540.
    KEGGimth:MTH1132.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09990 Genomic DNA. Translation: AAA73436.1 .
    AE000666 Genomic DNA. Translation: AAB85621.1 . Different initiation.
    J04540 Genomic DNA. Translation: AAB02353.1 .
    PIRi G69017.
    T45147.
    RefSeqi NP_276260.1. NC_000916.1.

    3D structure databases

    ProteinModelPortali P21111.
    SMRi P21111. Positions 4-443.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P21111. 1 interaction.
    STRINGi 187420.MTH1132.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAB85621 ; AAB85621 ; MTH_1132 .
    GeneIDi 1471540.
    KEGGi mth:MTH1132.

    Phylogenomic databases

    eggNOGi COG4054.
    KOi K00401.
    OMAi WALWNAY.

    Enzyme and pathway databases

    UniPathwayi UPA00646 ; UER00699 .
    BioCyci MetaCyc:MRTBMAUTO-MONOMER.
    MTHE187420:GJNM-1134-MONOMER.

    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. "Growth phase-dependent transcription of the genes that encode the two methyl coenzyme M reductase isoenzymes and N5-methyltetrahydromethanopterin:coenzyme M methyltransferase in Methanobacterium thermoautotrophicum delta H."
      Pihl T.D., Sharma S., Reeve J.N.
      J. Bacteriol. 176:6384-6391(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
    3. "A hydrogenase-linked gene in Methanobacterium thermoautotrophicum strain delta H encodes a polyferredoxin."
      Reeve J.N., Beckler G.S., Cram D.S., Hamilton P.T., Brown J.W., Krzycki J.A., Kolodziej A.F., Alex L., Orme-Johnson W.H., Walsh C.T.
      Proc. Natl. Acad. Sci. U.S.A. 86:3031-3035(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-146.
      Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
    4. "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 2-20.
      Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

    Entry informationi

    Entry nameiMCRY_METTH
    AccessioniPrimary (citable) accession number: P21111
    Secondary accession number(s): O27204
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 103 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways

    External Data

    Dasty 3