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P07961

- MCRA_METVA

UniProt

P07961 - MCRA_METVA

Protein

Methyl-coenzyme M reductase subunit alpha

Gene

mcrA

Organism
Methanococcus vannielii
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 Aug 1988)
      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 bindingi151 – 1511NickelBy 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 vannielii
    Taxonomic identifieri2187 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 553553Methyl-coenzyme M reductase subunit alphaPRO_0000147460Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei261 – 2611Pros-methylhistidineBy similarity
    Modified residuei275 – 27515-methylarginineBy similarity

    Keywords - PTMi

    Methylation

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP07961.
    SMRiP07961. Positions 7-552.
    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.

    P07961-1 [UniParc]FASTAAdd to Basket

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    MEAEKRLFLK ALKEKFEEDP KEKYTKFYTY GGWEQSVRKR EFVAANEKVL    50
    AEKRQGVPLY NPDIGVPLGQ RKLMPYKLSG TDSYCEGDDL HFMNNAAIQQ 100
    LWDDIRRTVV VGMDTAHSVL EKRLGVEVTP ETINEYMHTI NHALSGGAVV 150
    QEHMVEVHPS LAWDSYARIF TGDDELAAEL DSRFLIDINK LFPAEQAEAL 200
    KKAIGKKTYQ VSRVPSLVGR VCDGGTISRW SAMQIGMSFI TAYKLCAGEA 250
    ATADFSYASK HADVIQMGNA LPGRRARGPN EPGGIQFGIL SDVVQTTRVS 300
    DDPVEQSLEV VAAGAALYDQ IWLGAYMSGG VGFTQYATAA YTDDILDDFS 350
    YYALDYVEKK YGRMGTKATM DVVEDIASEV TLYSLEQYDE YPALLEDHFG 400
    GSQRAAVAAA ASGIGVCMAT GNSNAGVNGW YLSQILHKEY HSRLGFYGYD 450
    LQDQCGASNS LAIRNDESAP LELRGPNYPN YAMNVGHQGE YAGIAQAAHS 500
    ARGDAFAMSA LIKVAFADPM LVFDFSKPRK EFARGALREF DAAGERDVIL 550
    PAK 553
    Length:553
    Mass (Da):60,838
    Last modified:August 1, 1988 - v1
    Checksum:i7B91F2DDA4B98489
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16893 Genomic DNA. Translation: AAA72598.1.
    PIRiE27793.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16893 Genomic DNA. Translation: AAA72598.1 .
    PIRi E27793.

    3D structure databases

    ProteinModelPortali P07961.
    SMRi P07961. Positions 7-552.
    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. "Structure and expression of the genes, mcrBDCGA, which encode the subunits of component C of methyl coenzyme M reductase in Methanococcus vannielii."
      Cram D.S., Sherf B.A., Libby R.T., Mattaliano R.J., Ramachandran K.L., Reeve J.N.
      Proc. Natl. Acad. Sci. U.S.A. 84:3992-3996(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiMCRA_METVA
    AccessioniPrimary (citable) accession number: P07961
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    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