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P11559

- MCRA_METVO

UniProt

P11559 - MCRA_METVO

Protein

Methyl-coenzyme M reductase subunit alpha

Gene

mcrA

Organism
Methanococcus voltae
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 79 (01 Oct 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.

    Cofactori

    Binds 1 coenzyme F430 noncovalently per subunit. Coenzyme F430 is a yellow nickel porphinoid By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi152 – 1521NickelBy similarity

    GO - Molecular functioni

    1. coenzyme-B sulfoethylthiotransferase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. methanogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Methanogenesis

    Keywords - Ligandi

    Metal-binding, Nickel

    Enzyme and pathway databases

    UniPathwayiUPA00646; UER00699.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methyl-coenzyme M reductase subunit alpha (EC:2.8.4.1)
    Alternative name(s):
    Coenzyme-B sulfoethylthiotransferase alpha
    Gene namesi
    Name:mcrA
    OrganismiMethanococcus voltae
    Taxonomic identifieri2188 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 555555Methyl-coenzyme M reductase subunit alphaPRO_0000147461Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei262 – 2621Pros-methylhistidineBy similarity
    Modified residuei276 – 27615-methylarginineBy similarity

    Keywords - PTMi

    Methylation

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP11559.
    SMRiP11559. Positions 7-553.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Family and domain databases

    Gene3Di1.20.840.10. 1 hit.
    3.30.70.470. 1 hit.
    3.90.390.10. 1 hit.
    InterProiIPR022681. MCR_a/b_chain_a-bundle.
    IPR016212. Me_CoM_Rdtase_asu.
    IPR008924. Me_CoM_Rdtase_asu/bsu_C.
    IPR009047. Me_CoM_Rdtase_asu_C.
    IPR003183. Me_CoM_Rdtase_asu_N.
    IPR015811. Me_CoM_Rdtase_asu_N_sub1.
    IPR015823. Me_CoM_Rdtase_asu_N_sub2.
    IPR009024. Me_CoM_Rdtase_Fd-like_fold.
    [Graphical view]
    PfamiPF02249. MCR_alpha. 1 hit.
    PF02745. MCR_alpha_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000262. MCR_alpha. 1 hit.
    SUPFAMiSSF48081. SSF48081. 1 hit.
    SSF55088. SSF55088. 1 hit.
    TIGRFAMsiTIGR03256. met_CoM_red_alp. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P11559-1 [UniParc]FASTAAdd to Basket

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    MEAEKRLFLK ALKEKFEEDP KEKFTKFYTY GGWQQSARKQ EFVSENEKIV    50
    AEKRGGIPMY NPDIGVPLGQ RKLMPYKISN TDTYVEGDDL HFMNNAAIQQ 100
    LWDDIRRTVI VGMDTAHMVL EKRLGVEVTP ETINEYMHTI NHSLPGGAAV 150
    VQEHMVEVHP SLAWDCYAKI FTGDDELADE LDDRFVIDIN KLFPEEQAEA 200
    SKAAIGKKTY QVSRVPSLVG RVCDGGTISR WSAMQIGMSF ITAYKLCAGE 250
    AAIADFSYAA KHADVIQMGN ALLGRRARGP NELGGVRFGI LSDVVQTTRV 300
    SDDPVEQSLE VVATGAALYD QIWLGSYMSG GVGFTQYATA SYTDDILDDF 350
    SYYGYEYVEK KYGRCGTKAT MDVVEDIASE VTLYALEQYD EYPALLEDHF 400
    GGSQRAAVAA AAAGISVCMA TGNSNAGVNG WYLSQILHKE YHSRLGFYGY 450
    DLQDQCGASN SLAIRNDEAS PLELRGPNYP NYAMNVGHQG EYAGIAQSAH 500
    SARGDAFATN ALIKVAFADP SLVFDFSKPR KEIARGALRE FEAAGERDPI 550
    LPAKI 555
    Length:555
    Mass (Da):61,227
    Last modified:October 1, 1989 - v1
    Checksum:iDCBCE5DC91EA69D5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07793 Genomic DNA. Translation: CAA30633.1.
    PIRiS03261.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07793 Genomic DNA. Translation: CAA30633.1 .
    PIRi S03261.

    3D structure databases

    ProteinModelPortali P11559.
    SMRi P11559. Positions 7-553.
    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. 1 hit.
    3.30.70.470. 1 hit.
    3.90.390.10. 1 hit.
    InterProi IPR022681. MCR_a/b_chain_a-bundle.
    IPR016212. Me_CoM_Rdtase_asu.
    IPR008924. Me_CoM_Rdtase_asu/bsu_C.
    IPR009047. Me_CoM_Rdtase_asu_C.
    IPR003183. Me_CoM_Rdtase_asu_N.
    IPR015811. Me_CoM_Rdtase_asu_N_sub1.
    IPR015823. Me_CoM_Rdtase_asu_N_sub2.
    IPR009024. Me_CoM_Rdtase_Fd-like_fold.
    [Graphical view ]
    Pfami PF02249. MCR_alpha. 1 hit.
    PF02745. MCR_alpha_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000262. MCR_alpha. 1 hit.
    SUPFAMi SSF48081. SSF48081. 1 hit.
    SSF55088. SSF55088. 1 hit.
    TIGRFAMsi TIGR03256. met_CoM_red_alp. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Comparative analysis of genes encoding methyl coenzyme M reductase in methanogenic bacteria."
      Klein A., Allmansberger R., Bokranz M., Knaub S., Mueller B., Muth E.
      Mol. Gen. Genet. 213:409-420(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS.

    Entry informationi

    Entry nameiMCRA_METVO
    AccessioniPrimary (citable) accession number: P11559
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 79 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