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P21110

- MCRX_METTH

UniProt

P21110 - MCRX_METTH

Protein

Methyl-coenzyme M reductase II subunit alpha

Gene

mrtA

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 107 (01 Oct 2014)
      Sequence version 3 (30 May 2000)
      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 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

    BioCyciMetaCyc:MRTAMAUTO-MONOMER.
    MTHE187420:GJNM-1131-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
    Alternative name(s):
    Coenzyme-B sulfoethylthiotransferase alpha
    Gene namesi
    Name:mrtA
    Ordered Locus Names:MTH_1129
    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
    Chaini1 – 553553Methyl-coenzyme M reductase II subunit alphaPRO_0000147457Add
    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.

    Protein-protein interaction databases

    IntActiP21110. 2 interactions.
    STRINGi187420.MTH1129.

    Structurei

    3D structure databases

    ProteinModelPortaliP21110.
    SMRiP21110. Positions 6-551.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Phylogenomic databases

    eggNOGiCOG4058.
    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.

    P21110-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDEKKLFLTA LKKKFEVEDP 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 DIVQASRVSD 300
    DPAKISLEVI 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 SFDFTSPRKS IAAGALREFM PEGERDLIIP 550
    AGK 553
    Length:553
    Mass (Da):60,707
    Last modified:May 30, 2000 - v3
    Checksum:i8A3511715F7EFE00
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61L → H in AAA73439. (PubMed:7929010)Curated
    Sequence conflicti24 – 241Y → I in AAA73439. (PubMed:7929010)Curated
    Sequence conflicti168 – 1681I → V in AAA73439. (PubMed:7929010)Curated
    Sequence conflicti200 – 2001K → KEQLK(PubMed:7929010)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09990 Genomic DNA. Translation: AAA73439.1.
    AE000666 Genomic DNA. Translation: AAB85618.1.
    PIRiC69017.
    T45150.
    RefSeqiNP_276257.1. NC_000916.1.
    WP_010876753.1. NC_000916.1.

    Genome annotation databases

    EnsemblBacteriaiAAB85618; AAB85618; MTH_1129.
    GeneIDi1471537.
    KEGGimth:MTH1129.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09990 Genomic DNA. Translation: AAA73439.1 .
    AE000666 Genomic DNA. Translation: AAB85618.1 .
    PIRi C69017.
    T45150.
    RefSeqi NP_276257.1. NC_000916.1.
    WP_010876753.1. NC_000916.1.

    3D structure databases

    ProteinModelPortali P21110.
    SMRi P21110. Positions 6-551.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P21110. 2 interactions.
    STRINGi 187420.MTH1129.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAB85618 ; AAB85618 ; MTH_1129 .
    GeneIDi 1471537.
    KEGGi mth:MTH1129.

    Phylogenomic databases

    eggNOGi COG4058.
    KOi K00399.
    OMAi GHQPEYA.

    Enzyme and pathway databases

    UniPathwayi UPA00646 ; UER00699 .
    BioCyci MetaCyc:MRTAMAUTO-MONOMER.
    MTHE187420:GJNM-1131-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. "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. "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 1-15.
      Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

    Entry informationi

    Entry nameiMCRX_METTH
    AccessioniPrimary (citable) accession number: P21110
    Secondary accession number(s): O27201, Q50487
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 107 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways

    External Data

    Dasty 3