Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P12972

- MCRB_METFE

UniProt

P12972 - MCRB_METFE

Protein

Methyl-coenzyme M reductase subunit beta

Gene

mcrB

Organism
Methanothermus fervidus
Status
Reviewed - Annotation score: 3 out of 5- Protein predictedi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 73 (03 Sep 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 beta (EC:2.8.4.1)
    Alternative name(s):
    Coenzyme-B sulfoethylthiotransferase beta
    Gene namesi
    Name:mcrB
    OrganismiMethanothermus fervidus
    Taxonomic identifieri2180 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanothermaceaeMethanothermus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 438438Methyl-coenzyme M reductase subunit betaPRO_0000147463Add
    BLAST

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP12972.
    SMRiP12972. Positions 3-434.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    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.

    P12972-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKYEDKVDL YDDRGNLVEE QVPIEALSPL RNTAIKKIIH DIKRTVAVNL    50
    EGIENALRSA KVGGSGCHIP GRELDVDVID NAEAIAEKAK EMIQVEEGDD 100
    TVVELLHDGK RALVKVPSSR LESAAEYSVA PLVTASAFIQ SIIDVCDISI 150
    YDANMVKAAV LGRYPQSVEY VGGNIATMLD IPQKLEGPGY ALRNILVNHI 200
    VAATLKNTLQ AVALSSILEH TAMFEMGDAV GKFERLHLLG LAYQGLNADN 250
    LLYDLVKANG KDGTVGSVVE DVVERAKEDG VIKVEKELNG YKVYGTDDLA 300
    LWNAYAAAGL VAATIVNQGA ARAAQGVSST ILYDNDIIEF ERGLPGVDFG 350
    RAEGTAVGFS FFSHSIYGGG GPGIFNGNHI VTRHSKGFAI PCVAAAMALD 400
    AGTQMFSPEL TSGLIKDVFS KVDEFREPLK YVVELQPK 438
    Length:438
    Mass (Da):47,034
    Last modified:October 1, 1989 - v1
    Checksum:i76E0EE0DCB8CEC75
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03375 Genomic DNA. Translation: AAA72193.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03375 Genomic DNA. Translation: AAA72193.1 .

    3D structure databases

    ProteinModelPortali P12972.
    SMRi P12972. Positions 3-434.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00646 ; UER00699 .

    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. "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 nameiMCRB_METFE
    AccessioniPrimary (citable) accession number: P12972
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: September 3, 2014
    This is version 73 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