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P07955

- MCRB_METBF

UniProt

P07955 - MCRB_METBF

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Protein
Methyl-coenzyme M reductase subunit beta
Gene
mcrB, Mbar_A0897
Organism
Methanosarcina barkeri (strain Fusaro / DSM 804)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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: UniProtKB-EC

GO - Biological processi

  1. methanogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Methanogenesis

Enzyme and pathway databases

BioCyciMBAR269797:GHUW-911-MONOMER.
UniPathwayiUPA00646; UER00699.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-coenzyme M reductase subunit beta (EC:2.8.4.1)
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase beta
Gene namesi
Name:mcrB
Ordered Locus Names:Mbar_A0897
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 – 434433Methyl-coenzyme M reductase subunit beta
PRO_0000147462Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi269797.Mbar_A0897.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85
Beta strandi14 – 207
Helixi21 – 244
Turni26 – 283
Helixi30 – 4112
Beta strandi42 – 465
Helixi47 – 5610
Helixi76 – 783
Helixi79 – 9012
Beta strandi99 – 1035
Turni104 – 1074
Beta strandi108 – 1125
Helixi115 – 1195
Beta strandi121 – 1244
Helixi126 – 14217
Helixi147 – 1493
Helixi150 – 1589
Turni159 – 1635
Beta strandi164 – 1663
Beta strandi171 – 1733
Helixi179 – 1813
Helixi188 – 1903
Helixi194 – 2007
Turni201 – 2033
Helixi205 – 22218
Helixi229 – 24315
Helixi248 – 2569
Turni257 – 2593
Helixi262 – 27514
Beta strandi278 – 2847
Beta strandi290 – 2967
Helixi297 – 31923
Helixi322 – 3243
Helixi325 – 34016
Helixi345 – 3484
Helixi349 – 35911
Beta strandi362 – 3665
Helixi370 – 3723
Turni378 – 3803
Beta strandi382 – 3876
Helixi388 – 39710
Helixi406 – 41712
Helixi421 – 4244
Helixi426 – 4316

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E6YX-ray1.60B/E2-434[»]
ProteinModelPortaliP07955.
SMRiP07955. Positions 2-434.

Miscellaneous databases

EvolutionaryTraceiP07955.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG4054.
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.

P07955-1 [UniParc]FASTAAdd to Basket

« Hide

MSDTVDIYDD RGKLLESNVD IMSLAPTRNA AIQSIIMDTK RSVAVNLAGI    50
QGALASGKMG GKGRQILGRG LNYDIVGNAD AIAENVKKLV QVDEGDDTNV 100
IKVKGGKSLL IQSPKSRIIA GADFMSATTV GAAAVTQTIM DMFGTDPYDA 150
PIVKSAVWGS YPQTMDLMGG QVQGILSIPQ NNEGLGFSLR NIMANHVAAI 200
SNRNAMNASA LSSIYEQSGI FEMGGAVGMF ERHQLLGLAY QGLNANNLLY 250
DIVKENGKDG TIGTVIESVV RRAIEAGIIS VDKTAPSGYN FYKANDVPKW 300
NACAAVGTLA ATLVNCGAGR AAQNVSSTLL YFNDILEKET GLPGCDYGKV 350
EGTAVGFSFF SHSIYGGGGP GVFNGNHVVT RHSRGFAIPC VCAAVALDAG 400
TQMFSIESTS GLIGDVFGAI PEFREPIKAV AGVL 434
Length:434
Mass (Da):45,421
Last modified:January 23, 2007 - v3
Checksum:iA85044187FB78CB9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00158 Genomic DNA. Translation: CAA68353.1.
CP000099 Genomic DNA. Translation: AAZ69871.1.
PIRiA29525.
RefSeqiWP_011305920.1. NC_007355.1.
YP_304451.1. NC_007355.1.

Genome annotation databases

EnsemblBacteriaiAAZ69871; AAZ69871; Mbar_A0897.
GeneIDi3625942.
KEGGimba:Mbar_A0897.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00158 Genomic DNA. Translation: CAA68353.1 .
CP000099 Genomic DNA. Translation: AAZ69871.1 .
PIRi A29525.
RefSeqi WP_011305920.1. NC_007355.1.
YP_304451.1. 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 B/E 2-434 [» ]
ProteinModelPortali P07955.
SMRi P07955. Positions 2-434.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 269797.Mbar_A0897.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAZ69871 ; AAZ69871 ; Mbar_A0897 .
GeneIDi 3625942.
KEGGi mba:Mbar_A0897.

Phylogenomic databases

eggNOGi COG4054.
HOGENOMi HOG000225842.
KOi K00401.
OMAi FREPLKY.

Enzyme and pathway databases

UniPathwayi UPA00646 ; UER00699 .
BioCyci MBAR269797:GHUW-911-MONOMER.

Miscellaneous databases

EvolutionaryTracei P07955.

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

« Hide 'large scale' publications
  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), SUBUNIT.

Entry informationi

Entry nameiMCRB_METBF
AccessioniPrimary (citable) accession number: P07955
Secondary accession number(s): Q46E21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 107 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

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

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