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P11558

- MCRA_METTM

UniProt

P11558 - MCRA_METTM

Protein

Methyl-coenzyme M reductase I subunit alpha

Gene

mcrA

Organism
Methanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (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.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi147 – 1471Nickel

    GO - Molecular functioni

    1. coenzyme-B sulfoethylthiotransferase activity Source: MENGO
    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-1552-MONOMER.
    UniPathwayiUPA00646; UER00699.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methyl-coenzyme M reductase I subunit alpha (EC:2.8.4.1)
    Short name:
    MCR I alpha
    Alternative name(s):
    Coenzyme-B sulfoethylthiotransferase alpha
    Gene namesi
    Name:mcrA
    Ordered Locus Names:MTBMA_c15480
    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
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 550549Methyl-coenzyme M reductase I subunit alphaPRO_0000147456Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei257 – 2571Pros-methylhistidine
    Modified residuei271 – 27115-methylarginine
    Modified residuei400 – 40012-methylglutamine
    Modified residuei445 – 44511-thioglycine
    Modified residuei452 – 4521S-methylcysteine

    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.

    Structurei

    Secondary structure

    1
    550
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 137
    Helixi30 – 334
    Helixi35 – 5117
    Beta strandi60 – 623
    Beta strandi71 – 744
    Beta strandi80 – 823
    Helixi83 – 864
    Helixi88 – 903
    Helixi92 – 10211
    Beta strandi104 – 1096
    Helixi110 – 1189
    Helixi126 – 13914
    Turni140 – 1423
    Helixi155 – 1584
    Beta strandi162 – 1687
    Helixi170 – 1756
    Helixi178 – 1803
    Helixi184 – 1874
    Helixi190 – 20011
    Beta strandi204 – 2096
    Helixi212 – 2176
    Helixi222 – 23918
    Helixi246 – 25611
    Turni257 – 2593
    Helixi269 – 2713
    Beta strandi275 – 2773
    Helixi278 – 2803
    Helixi283 – 2897
    Helixi292 – 2954
    Helixi300 – 31617
    Helixi317 – 3237
    Helixi331 – 3355
    Turni336 – 3383
    Helixi342 – 35716
    Helixi367 – 38721
    Helixi389 – 3946
    Helixi398 – 41720
    Helixi420 – 43819
    Helixi448 – 45710
    Turni462 – 4643
    Helixi468 – 4703
    Helixi476 – 4783
    Beta strandi482 – 4843
    Helixi485 – 49915
    Helixi507 – 5126
    Beta strandi518 – 5203
    Helixi525 – 5339
    Helixi544 – 5463

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HBMX-ray1.80A/D2-550[»]
    1HBNX-ray1.16A/D2-550[»]
    1HBOX-ray1.78A/D2-550[»]
    1HBUX-ray1.90A/D2-550[»]
    1MROX-ray1.16A/D2-549[»]
    3M1VX-ray1.45A/D2-550[»]
    3M2RX-ray1.30A/D2-550[»]
    3M2UX-ray1.40A/D2-550[»]
    3M2VX-ray1.80A/D2-550[»]
    3M30X-ray1.45A/D2-550[»]
    3M32X-ray1.35A/D2-550[»]
    3POTX-ray1.20A/D1-550[»]
    ProteinModelPortaliP11558.
    SMRiP11558. Positions 2-549.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11558.

    Family & Domainsi

    Phylogenomic databases

    HOGENOMiHOG000225809.
    KOiK00399.
    OMAiMSMISAY.

    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.

    P11558-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADKLFINAL KKKFEESPEE KKTTFYTLGG WKQSERKTEF VNAGKEVAAK    50
    RGIPQYNPDI GTPLGQRVLM PYQVSTTDTY VEGDDLHFVN NAAMQQMWDD 100
    IRRTVIVGLN HAHAVIEKRL GKEVTPETIT HYLETVNHAM PGAAVVQEHM 150
    VETHPALVAD SYVKVFTGND EIADEIDPAF VIDINKQFPE DQAETLKAEV 200
    GDGIWQVVRI PTIVSRTCDG ATTSRWSAMQ IGMSMISAYK QAAGEAATGD 250
    FAYAAKHAEV IHMGTYLPVR RARGENEPGG VPFGYLADIC QSSRVNYEDP 300
    VRVSLDVVAT GAMLYDQIWL GSYMSGGVGF TQYATAAYTD NILDDFTYFG 350
    KEYVEDKYGL CEAPNNMDTV LDVATEVTFY GLEQYEEYPA LLEDQFGGSQ 400
    RAAVVAAAAG CSTAFATGNA QTGLSGWYLS MYLHKEQHSR LGFYGYDLQD 450
    QCGASNVFSI RGDEGLPLEL RGPNYPNYAM NVGHQGEYAG ISQAPHAARG 500
    DAFVFNPLVK IAFADDNLVF DFTNVRGEFA KGALREFEPA GERALITPAK 550
    Length:550
    Mass (Da):60,511
    Last modified:January 23, 2007 - v3
    Checksum:iD55A724B6CA9EFEE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07794 Genomic DNA. Translation: CAA30639.1.
    CP001710 Genomic DNA. Translation: ADL59127.1.
    RefSeqiYP_003850440.1. NC_014408.1.

    Genome annotation databases

    EnsemblBacteriaiADL59127; ADL59127; MTBMA_c15480.
    GeneIDi9705257.
    KEGGimmg:MTBMA_c15480.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07794 Genomic DNA. Translation: CAA30639.1 .
    CP001710 Genomic DNA. Translation: ADL59127.1 .
    RefSeqi YP_003850440.1. NC_014408.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HBM X-ray 1.80 A/D 2-550 [» ]
    1HBN X-ray 1.16 A/D 2-550 [» ]
    1HBO X-ray 1.78 A/D 2-550 [» ]
    1HBU X-ray 1.90 A/D 2-550 [» ]
    1MRO X-ray 1.16 A/D 2-549 [» ]
    3M1V X-ray 1.45 A/D 2-550 [» ]
    3M2R X-ray 1.30 A/D 2-550 [» ]
    3M2U X-ray 1.40 A/D 2-550 [» ]
    3M2V X-ray 1.80 A/D 2-550 [» ]
    3M30 X-ray 1.45 A/D 2-550 [» ]
    3M32 X-ray 1.35 A/D 2-550 [» ]
    3POT X-ray 1.20 A/D 1-550 [» ]
    ProteinModelPortali P11558.
    SMRi P11558. Positions 2-549.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADL59127 ; ADL59127 ; MTBMA_c15480 .
    GeneIDi 9705257.
    KEGGi mmg:MTBMA_c15480.

    Phylogenomic databases

    HOGENOMi HOG000225809.
    KOi K00399.
    OMAi MSMISAY.

    Enzyme and pathway databases

    UniPathwayi UPA00646 ; UER00699 .
    BioCyci MMAR79929:GH5J-1552-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P11558.

    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. "Cloning and characterization of the methyl coenzyme M reductase genes from Methanobacterium thermoautotrophicum."
      Bokranz M., Baeumner G., Allmansberger R., Ankel-Fuchs D., Klein A.
      J. Bacteriol. 170:568-577(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
    2. "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.
    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 2-19.
      Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
    4. "The biosynthesis of methylated amino acids in the active site region of methyl-coenzyme M reductase."
      Selmer T., Kahnt J., Goubeaud M., Shima S., Grabarse W., Ermler U., Thauer R.K.
      J. Biol. Chem. 275:3755-3760(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: POST-TRANSLATIONAL MODIFICATIONS.
      Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
    5. "Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation."
      Ermler U., Grabarse W., Shima S., Goubeaud M., Thauer R.K.
      Science 278:1457-1462(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
      Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
    6. "On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding."
      Grabarse W., Mahlert F., Duin E.C., Goubeaud M., Shima S., Thauer R.K., Lamzin V., Ermler U.
      J. Mol. Biol. 309:315-330(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS).
      Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.

    Entry informationi

    Entry nameiMCRA_METTM
    AccessioniPrimary (citable) accession number: P11558
    Secondary accession number(s): D9PY29
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 106 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, Direct protein sequencing

    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