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)

P12971

- MCRA_METFE

UniProt

P12971 - MCRA_METFE

Protein

Methyl-coenzyme M reductase subunit alpha

Gene

mcrA

Organism
Methanothermus fervidus
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 78 (01 Oct 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.

    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

    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
    OrganismiMethanothermus fervidus
    Taxonomic identifieri2180 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanothermaceaeMethanothermus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 555555Methyl-coenzyme M reductase subunit alphaPRO_0000147450Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Methylation

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP12971.
    SMRiP12971. 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.

    P12971-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEERKKLFV DALRKKFKEE PKERKTTFYT LGGWKQSERK KEFVEYGKKV    50
    AKERGIPAYN PDIGTPLGQR VLMPYQVSTT DTFVEGDDLH FVNNLAMQQF 100
    WDDIRRTVIV GLNHAHRILE RSLGKEVTPE TINHYLETVN HAMPGAAVVQ 150
    EHMVETHPGL TADSYVKVFT GNDELADEIE SCYLIDINKQ FPEHQAEQLK 200
    KAIGHTIWQA VRIPTIVSRT CDGATTSRWS AMQIGMSMIS AYKQAAGEAA 250
    TADFAYAAKH AEVIHLGTFL PVRRARGENE LGGVPFGFLA DIVQSSRVHY 300
    EDPVRVALDV VASGAMLYDQ IWLGSYMSGG VGFTQYATAS YTDNILDDFT 350
    YYGKEYVEDK YGGLAEAPHD FDTILDVATE VTLYSLDQYE EYPTLMEDHF 400
    GGSQRAAIAA AASGCSTAFA AGNAQAGLSG WYLSQILHKE CHARLGFYGY 450
    DLQDQCGAAN TYSIRSDEGL PAELRGPNYP NYAMNVGHLG EYAGIVQAAH 500
    IARGDADSLN PLVKVAFADD NLPFDWTNPR GEFAKGALRE FEPEGERDLI 550
    RPAGK 555
    Length:555
    Mass (Da):61,550
    Last modified:October 1, 1989 - v1
    Checksum:iC2517AB56DA53D72
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03375 Genomic DNA. Translation: AAA72197.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03375 Genomic DNA. Translation: AAA72197.1 .

    3D structure databases

    ProteinModelPortali P12971.
    SMRi P12971. 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. "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 nameiMCRA_METFE
    AccessioniPrimary (citable) accession number: P12971
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 78 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