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P11560

- MCRB_METTM

UniProt

P11560 - MCRB_METTM

Protein

Methyl-coenzyme M reductase I subunit beta

Gene

mcrB

Organism
Methanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (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.

    Pathwayi

    GO - Molecular functioni

    1. coenzyme-B sulfoethylthiotransferase activity Source: MENGO

    GO - Biological processi

    1. methanogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Methanogenesis

    Enzyme and pathway databases

    BioCyciMMAR79929:GH5J-1556-MONOMER.
    UniPathwayiUPA00646; UER00699.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methyl-coenzyme M reductase I subunit beta (EC:2.8.4.1)
    Short name:
    MCR I beta
    Alternative name(s):
    Coenzyme-B sulfoethylthiotransferase beta
    Gene namesi
    Name:mcrB
    Ordered Locus Names:MTBMA_c15520
    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 – 443442Methyl-coenzyme M reductase I subunit betaPRO_0000147468Add
    BLAST

    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
    443
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 115
    Beta strandi17 – 237
    Helixi24 – 274
    Turni29 – 313
    Helixi33 – 4412
    Beta strandi45 – 495
    Helixi50 – 5910
    Helixi79 – 813
    Helixi82 – 9312
    Beta strandi102 – 1065
    Helixi107 – 1093
    Beta strandi111 – 1155
    Helixi118 – 1225
    Beta strandi125 – 1273
    Helixi129 – 14618
    Turni150 – 1523
    Helixi153 – 1619
    Turni162 – 1665
    Beta strandi167 – 1693
    Beta strandi174 – 1763
    Helixi182 – 1843
    Helixi191 – 1933
    Helixi197 – 2037
    Turni204 – 2063
    Helixi208 – 22518
    Turni226 – 2294
    Helixi231 – 2333
    Helixi234 – 24512
    Helixi248 – 2503
    Helixi251 – 2599
    Turni260 – 2623
    Helixi265 – 27814
    Beta strandi283 – 2886
    Beta strandi291 – 2955
    Helixi299 – 32123
    Helixi324 – 3263
    Helixi327 – 34216
    Helixi347 – 3504
    Helixi351 – 36111
    Beta strandi364 – 3685
    Helixi372 – 3743
    Turni380 – 3823
    Beta strandi384 – 3896
    Helixi390 – 39910
    Helixi408 – 4114
    Helixi413 – 4197
    Helixi423 – 4264
    Helixi428 – 43912
    Turni440 – 4423

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HBMX-ray1.80B/E2-443[»]
    1HBNX-ray1.16B/E2-443[»]
    1HBOX-ray1.78B/E2-443[»]
    1HBUX-ray1.90B/E2-443[»]
    1MROX-ray1.16B/E2-443[»]
    3M1VX-ray1.45B/E2-443[»]
    3M2RX-ray1.30B/E2-443[»]
    3M2UX-ray1.40B/E2-443[»]
    3M2VX-ray1.80B/E2-443[»]
    3M30X-ray1.45B/E2-443[»]
    3M32X-ray1.35B/E2-443[»]
    3POTX-ray1.20B/E1-443[»]
    ProteinModelPortaliP11560.
    SMRiP11560. Positions 2-443.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11560.

    Family & Domainsi

    Phylogenomic databases

    HOGENOMiHOG000225842.
    KOiK00401.
    OMAiFREPLKY.

    Family and domain databases

    Gene3Di1.20.840.10. 2 hits.
    3.30.70.470. 1 hit.
    InterProiIPR022681. MCR_a/b_chain_a-bundle.
    IPR008924. Me_CoM_Rdtase_asu/bsu_C.
    IPR015823. Me_CoM_Rdtase_asu_N_sub2.
    IPR003179. Me_CoM_Rdtase_bsu.
    IPR022679. Me_CoM_Rdtase_bsu_C.
    IPR022680. Me_CoM_Rdtase_bsu_N.
    IPR009024. Me_CoM_Rdtase_Fd-like_fold.
    [Graphical view]
    PfamiPF02241. MCR_beta. 1 hit.
    PF02783. MCR_beta_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000263. Meth_CoM_rd_beta. 1 hit.
    SUPFAMiSSF48081. SSF48081. 1 hit.
    SSF55088. SSF55088. 1 hit.
    TIGRFAMsiTIGR03257. met_CoM_red_bet. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P11560-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKFEDKVDL YDDRGNLVEE QVPLEALSPL RNPAIKSIVQ GIKRTVAVNL    50
    EGIENALKTA KVGGPACKIM GRELDLDIVG NAESIAAAAK EMIQVTEDDD 100
    TNVELLGGGK RALVQVPSAR FDVAAEYSAA PLVTATAFVQ AIINEFDVSM 150
    YDANMVKAAV LGRYPQSVEY MGANIATMLD IPQKLEGPGY ALRNIMVNHV 200
    VAATLKNTLQ AAALSTILEQ TAMFEMGDAV GAFERMHLLG LAYQGMNADN 250
    LVFDLVKANG KEGTVGSVIA DLVERALEDG VIKVEKELTD YKVYGTDDLA 300
    MWNAYAAAGL MAATMVNQGA ARAAQGVSST LLYYNDLIEF ETGLPSVDFG 350
    KVEGTAVGFS FFSHSIYGGG GPGIFNGNHI VTRHSKGFAI PCVAAAMALD 400
    AGTQMFSPEA TSGLIKEVFS QVDEFREPLK YVVEAAAEIK NEI 443
    Length:443
    Mass (Da):47,240
    Last modified:January 23, 2007 - v3
    Checksum:i1237E83E405E6D6B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07794 Genomic DNA. Translation: CAA30635.1.
    CP001710 Genomic DNA. Translation: ADL59131.1.
    PIRiA28544.
    RefSeqiYP_003850444.1. NC_014408.1.

    Genome annotation databases

    EnsemblBacteriaiADL59131; ADL59131; MTBMA_c15520.
    GeneIDi9705261.
    KEGGimmg:MTBMA_c15520.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07794 Genomic DNA. Translation: CAA30635.1 .
    CP001710 Genomic DNA. Translation: ADL59131.1 .
    PIRi A28544.
    RefSeqi YP_003850444.1. 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 B/E 2-443 [» ]
    1HBN X-ray 1.16 B/E 2-443 [» ]
    1HBO X-ray 1.78 B/E 2-443 [» ]
    1HBU X-ray 1.90 B/E 2-443 [» ]
    1MRO X-ray 1.16 B/E 2-443 [» ]
    3M1V X-ray 1.45 B/E 2-443 [» ]
    3M2R X-ray 1.30 B/E 2-443 [» ]
    3M2U X-ray 1.40 B/E 2-443 [» ]
    3M2V X-ray 1.80 B/E 2-443 [» ]
    3M30 X-ray 1.45 B/E 2-443 [» ]
    3M32 X-ray 1.35 B/E 2-443 [» ]
    3POT X-ray 1.20 B/E 1-443 [» ]
    ProteinModelPortali P11560.
    SMRi P11560. Positions 2-443.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADL59131 ; ADL59131 ; MTBMA_c15520 .
    GeneIDi 9705261.
    KEGGi mmg:MTBMA_c15520.

    Phylogenomic databases

    HOGENOMi HOG000225842.
    KOi K00401.
    OMAi FREPLKY.

    Enzyme and pathway databases

    UniPathwayi UPA00646 ; UER00699 .
    BioCyci MMAR79929:GH5J-1556-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P11560.

    Family and domain databases

    Gene3Di 1.20.840.10. 2 hits.
    3.30.70.470. 1 hit.
    InterProi IPR022681. MCR_a/b_chain_a-bundle.
    IPR008924. Me_CoM_Rdtase_asu/bsu_C.
    IPR015823. Me_CoM_Rdtase_asu_N_sub2.
    IPR003179. Me_CoM_Rdtase_bsu.
    IPR022679. Me_CoM_Rdtase_bsu_C.
    IPR022680. Me_CoM_Rdtase_bsu_N.
    IPR009024. Me_CoM_Rdtase_Fd-like_fold.
    [Graphical view ]
    Pfami PF02241. MCR_beta. 1 hit.
    PF02783. MCR_beta_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000263. Meth_CoM_rd_beta. 1 hit.
    SUPFAMi SSF48081. SSF48081. 1 hit.
    SSF55088. SSF55088. 1 hit.
    TIGRFAMsi TIGR03257. met_CoM_red_bet. 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 2-21.
      Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
    4. "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.
    5. "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 nameiMCRB_METTM
    AccessioniPrimary (citable) accession number: P11560
    Secondary accession number(s): D9PY33
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 100 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