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P07955

- MCRB_METBF

UniProt

P07955 - MCRB_METBF

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Protein

Methyl-coenzyme M reductase subunit beta

Gene

mcrB

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 betaPRO_0000147462Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi269797.Mbar_A0897.

Structurei

Secondary structure

1
434
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Beta strandi14 – 207Combined sources
Helixi21 – 244Combined sources
Turni26 – 283Combined sources
Helixi30 – 4112Combined sources
Beta strandi42 – 465Combined sources
Helixi47 – 5610Combined sources
Helixi76 – 783Combined sources
Helixi79 – 9012Combined sources
Beta strandi99 – 1035Combined sources
Turni104 – 1074Combined sources
Beta strandi108 – 1125Combined sources
Helixi115 – 1195Combined sources
Beta strandi121 – 1244Combined sources
Helixi126 – 14217Combined sources
Helixi147 – 1493Combined sources
Helixi150 – 1589Combined sources
Turni159 – 1635Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi171 – 1733Combined sources
Helixi179 – 1813Combined sources
Helixi188 – 1903Combined sources
Helixi194 – 2007Combined sources
Turni201 – 2033Combined sources
Helixi205 – 22218Combined sources
Helixi229 – 24315Combined sources
Helixi248 – 2569Combined sources
Turni257 – 2593Combined sources
Helixi262 – 27514Combined sources
Beta strandi278 – 2847Combined sources
Beta strandi290 – 2967Combined sources
Helixi297 – 31923Combined sources
Helixi322 – 3243Combined sources
Helixi325 – 34016Combined sources
Helixi345 – 3484Combined sources
Helixi349 – 35911Combined sources
Beta strandi362 – 3665Combined sources
Helixi370 – 3723Combined sources
Turni378 – 3803Combined sources
Beta strandi382 – 3876Combined sources
Helixi388 – 39710Combined sources
Helixi406 – 41712Combined sources
Helixi421 – 4244Combined sources
Helixi426 – 4316Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E6YX-ray1.60B/E2-434[»]
ProteinModelPortaliP07955.
SMRiP07955. Positions 2-434.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MSDTVDIYDD RGKLLESNVD IMSLAPTRNA AIQSIIMDTK RSVAVNLAGI
60 70 80 90 100
QGALASGKMG GKGRQILGRG LNYDIVGNAD AIAENVKKLV QVDEGDDTNV
110 120 130 140 150
IKVKGGKSLL IQSPKSRIIA GADFMSATTV GAAAVTQTIM DMFGTDPYDA
160 170 180 190 200
PIVKSAVWGS YPQTMDLMGG QVQGILSIPQ NNEGLGFSLR NIMANHVAAI
210 220 230 240 250
SNRNAMNASA LSSIYEQSGI FEMGGAVGMF ERHQLLGLAY QGLNANNLLY
260 270 280 290 300
DIVKENGKDG TIGTVIESVV RRAIEAGIIS VDKTAPSGYN FYKANDVPKW
310 320 330 340 350
NACAAVGTLA ATLVNCGAGR AAQNVSSTLL YFNDILEKET GLPGCDYGKV
360 370 380 390 400
EGTAVGFSFF SHSIYGGGGP GVFNGNHVVT RHSRGFAIPC VCAAVALDAG
410 420 430
TQMFSIESTS GLIGDVFGAI PEFREPIKAV AGVL
Length:434
Mass (Da):45,421
Last modified:January 23, 2007 - v3
Checksum:iA85044187FB78CB9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 109 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