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P58815

- MCRX_METTM

UniProt

P58815 - MCRX_METTM

Protein

Methyl-coenzyme M reductase II subunit alpha

Gene

mrtA

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 50 (01 Oct 2014)
      Sequence version 2 (30 Nov 2010)
      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.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi150 – 1501NickelBy 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

    BioCyciMMAR79929:GH5J-1516-MONOMER.
    UniPathwayiUPA00646; UER00699.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methyl-coenzyme M reductase II subunit alpha (EC:2.8.4.1)
    Short name:
    MCR II alpha
    Gene namesi
    Name:mrtA
    Ordered Locus Names:MTBMA_c15120
    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
    Chaini1 – 553553Methyl-coenzyme M reductase II subunit alphaPRO_0000147458Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei260 – 2601Pros-methylhistidineBy similarity
    Modified residuei274 – 27415-methylarginineBy similarity

    Keywords - PTMi

    Methylation

    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.

    Family & Domainsi

    Phylogenomic databases

    HOGENOMiHOG000225809.
    KOiK00399.
    OMAiGHQPEYA.

    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.

    P58815-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDEKKLFLKA LKKKFEGEDP DEKYTNFYCF GGWEQSARKK EFTEYAKKAA    50
    EKRGGIPFYN PDIGVPLGQR KLMAYRVSGT DAYVEGDDLH FVNNAAIQQM 100
    VDDIKRTVIV GMDTAHAVLE KRLGVEVTPE TINEYMEAIN HALPGGAVVQ 150
    EHMVEVHPGL VEDCYAKIFT GDDNLADELD KRILIDINKE FPEEQAEQLK 200
    SYIGNRTYQV NRVPTIVVRT CDGGTVSRWS AMQIGMSFIS AYKLCAGEAA 250
    IADFSYAAKH ADVIEMGTIM PARRARGPNE PGGVAFGTFA DIVQTSRVSD 300
    DPANVSLEVI AGAAALYDQV WLGSYMSGGV GFTQYATAAY TDDILDDFVY 350
    YGMEYVDDKY GICGTKPTMD VVRDISTEVT LYSLEQYEEY PTLLEDHFGG 400
    SQRAAVAAAA AGCSTAFATG NSNAGINGWY LSQILHKEAH SRLGFYGYDL 450
    QDQCGASNSL SIRSDEGLIH ELRGPNYPNY AMNVGHQPEY AGIAQAPHAA 500
    RGDAFCTNPL IKVAFADKDL AFDFTSPRKS IAAGALREFM PEGERDLIIP 550
    AGK 553
    Length:553
    Mass (Da):60,678
    Last modified:November 30, 2010 - v2
    Checksum:i94CC0D641E7C8271
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21D → L AA sequence (PubMed:2269306)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001710 Genomic DNA. Translation: ADL59091.1.
    RefSeqiYP_003850404.1. NC_014408.1.

    Genome annotation databases

    EnsemblBacteriaiADL59091; ADL59091; MTBMA_c15120.
    GeneIDi9705221.
    KEGGimmg:MTBMA_c15120.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001710 Genomic DNA. Translation: ADL59091.1 .
    RefSeqi YP_003850404.1. NC_014408.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADL59091 ; ADL59091 ; MTBMA_c15120 .
    GeneIDi 9705221.
    KEGGi mmg:MTBMA_c15120.

    Phylogenomic databases

    HOGENOMi HOG000225809.
    KOi K00399.
    OMAi GHQPEYA.

    Enzyme and pathway databases

    UniPathwayi UPA00646 ; UER00699 .
    BioCyci MMAR79929:GH5J-1516-MONOMER.

    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. "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.
    2. "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 1-14.
      Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.

    Entry informationi

    Entry nameiMCRX_METTM
    AccessioniPrimary (citable) accession number: P58815
    Secondary accession number(s): D9PXZ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2002
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 50 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways

    External Data

    Dasty 3