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P07962

- MCRA_METBF

UniProt

P07962 - MCRA_METBF

Protein

Methyl-coenzyme M reductase subunit alpha

Gene

mcrA

Organism
Methanosarcina barkeri (strain Fusaro / DSM 804)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi161 – 1611Nickel

    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

    BioCyciMBAR269797:GHUW-907-MONOMER.
    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
    Ordered Locus Names:Mbar_A0893
    OrganismiMethanosarcina barkeri (strain Fusaro / DSM 804)
    Taxonomic identifieri269797 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
    ProteomesiUP000008156: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 570569Methyl-coenzyme M reductase subunit alphaPRO_0000147449Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei271 – 2711Pros-methylhistidine1 Publication
    Modified residuei285 – 28515-methylarginine1 Publication
    Modified residuei465 – 46511-thioglycine
    Modified residuei472 – 4721S-methylcysteine1 Publication

    Keywords - PTMi

    Methylation

    Interactioni

    Subunit structurei

    Hexamer of two alpha, two beta, and two gamma chains.1 Publication

    Protein-protein interaction databases

    STRINGi269797.Mbar_A0893.

    Structurei

    Secondary structure

    1
    570
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1715
    Helixi43 – 453
    Helixi47 – 6317
    Helixi70 – 723
    Beta strandi73 – 764
    Beta strandi86 – 883
    Helixi97 – 1004
    Helixi102 – 1043
    Helixi106 – 11611
    Beta strandi118 – 1236
    Helixi124 – 13411
    Helixi140 – 15314
    Turni154 – 1563
    Helixi169 – 1713
    Beta strandi176 – 1827
    Helixi184 – 1874
    Helixi192 – 1943
    Helixi198 – 2014
    Helixi204 – 21411
    Beta strandi218 – 2236
    Helixi226 – 2316
    Helixi236 – 25217
    Helixi260 – 27011
    Turni271 – 2733
    Helixi283 – 2853
    Beta strandi289 – 2913
    Helixi292 – 2943
    Helixi297 – 3037
    Helixi306 – 3094
    Helixi313 – 33018
    Helixi331 – 3366
    Helixi344 – 3485
    Turni349 – 3513
    Helixi355 – 37016
    Beta strandi379 – 3813
    Helixi387 – 40721
    Helixi409 – 4146
    Helixi418 – 43720
    Helixi440 – 45819
    Helixi468 – 4714
    Helixi473 – 4775
    Turni482 – 4843
    Turni488 – 4903
    Helixi496 – 4983
    Beta strandi502 – 5043
    Helixi505 – 51713
    Turni518 – 5203
    Helixi527 – 5326
    Beta strandi538 – 5403
    Helixi545 – 5539
    Helixi564 – 5663

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E6YX-ray1.60A/D2-570[»]
    ProteinModelPortaliP07962.
    SMRiP07962. Positions 2-569.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07962.

    Family & Domainsi

    Phylogenomic databases

    eggNOGiCOG4058.
    HOGENOMiHOG000225809.
    KOiK00399.
    OMAiAHSARGD.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P07962-1 [UniParc]FASTAAdd to Basket

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    MAADIFSKFK KDMEVKFAQE FGSNKQTGGD ITDKTAKFLR LGPEQDPRKV    50
    EMIKAGKEIA EKRGIAFYNP MMHSGAPLGQ RAITPYTISG TDIVCEPDDL 100
    HYVNNAAMQQ MWDDIRRTCI VGLDMAHETL EKRLGKEVTP ETINHYLEVL 150
    NHAMPGAAVV QEMMVETHPA LVDDCYVKVF TGDDALADEI DKQFLIDINK 200
    EFSEEQAAQI KASIGKTSWQ AIHIPTIVSR TTDGAQTSRW AAMQIGMSFI 250
    SAYAMCAGEA AVADLSFAAK HAALVSMGEM LPARRARGPN EPGGLSFGHL 300
    SDIVQTSRVS EDPAKIALEV VGAGCMLYDQ IWLGSYMSGG VGFTQYATAA 350
    YTDDILDNNT YYDVDYINDK YNGAATVGKD NKVKASLEVV KDIATESTLY 400
    GIETYEKFPT ALEDHFGGSQ RATVLAAAAG VACSLATGNA NAGLSGWYLS 450
    MYLHKEAWGR LGFFGFDLQD QCGATNVLSY QGDEGLPDEL RGPNYPNYAM 500
    NVGHQGGYAG IAQAAHSGRG DAFTVNPLLK VCFADDLLPF NFAEPRREFG 550
    RGAIREFVPA GERSLVIPAK 570
    Length:570
    Mass (Da):61,962
    Last modified:January 23, 2007 - v3
    Checksum:i301E10CE7D449C76
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00158 Genomic DNA. Translation: CAA68357.1.
    CP000099 Genomic DNA. Translation: AAZ69867.1.
    PIRiE29525.
    RefSeqiWP_011305916.1. NC_007355.1.
    YP_304447.1. NC_007355.1.

    Genome annotation databases

    EnsemblBacteriaiAAZ69867; AAZ69867; Mbar_A0893.
    GeneIDi3625938.
    KEGGimba:Mbar_A0893.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00158 Genomic DNA. Translation: CAA68357.1 .
    CP000099 Genomic DNA. Translation: AAZ69867.1 .
    PIRi E29525.
    RefSeqi WP_011305916.1. NC_007355.1.
    YP_304447.1. NC_007355.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E6Y X-ray 1.60 A/D 2-570 [» ]
    ProteinModelPortali P07962.
    SMRi P07962. Positions 2-569.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 269797.Mbar_A0893.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAZ69867 ; AAZ69867 ; Mbar_A0893 .
    GeneIDi 3625938.
    KEGGi mba:Mbar_A0893.

    Phylogenomic databases

    eggNOGi COG4058.
    HOGENOMi HOG000225809.
    KOi K00399.
    OMAi AHSARGD.

    Enzyme and pathway databases

    UniPathwayi UPA00646 ; UER00699 .
    BioCyci MBAR269797:GHUW-907-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P07962.

    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. "Nucleotide sequence of the methyl coenzyme M reductase gene cluster from Methanosarcina barkeri."
      Bokranz M., Klein A.
      Nucleic Acids Res. 15:4350-4351(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes."
      Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.
      J. Bacteriol. 188:7922-7931(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Fusaro / DSM 804.
    3. "Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation."
      Grabarse W., Mahlert F., Shima S., Thauer R.K., Ermler U.
      J. Mol. Biol. 303:329-344(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH COENZYME F430, COFACTOR, METHYLATION AT HIS-271, METHYLATION AT ARG-285, METHYLATION AT CYS-472, THIOLATION AT GLY-465, SUBUNIT.

    Entry informationi

    Entry nameiMCRA_METBF
    AccessioniPrimary (citable) accession number: P07962
    Secondary accession number(s): Q46E25
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 113 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3