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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: 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.

Pathway:imethyl-coenzyme M reduction

This protein is involved in step 1 of the subpathway that synthesizes methane from methyl-coenzyme M.
Proteins known to be involved in this subpathway in this organism are:
  1. Methyl-coenzyme M reductase II subunit alpha (mrtA), Methyl-coenzyme M reductase I subunit beta (mcrB), Methyl-coenzyme M reductase II subunit gamma (mrtG), Methyl-coenzyme M reductase I subunit alpha (mcrA), Methyl-coenzyme M reductase I subunit gamma (mcrG)
This subpathway is part of the pathway methyl-coenzyme M reduction, which is itself part of One-carbon metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes methane from methyl-coenzyme M, the pathway methyl-coenzyme M reduction and in One-carbon metabolism.

GO - Molecular functioni

  • coenzyme-B sulfoethylthiotransferase activity Source: MENGO

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Methanogenesis

Enzyme and pathway databases

BioCyciMMAR79929:GH5J-1556-MONOMER.
BRENDAi2.8.4.1. 7427.
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 Componenti: 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.

Protein-protein interaction databases

STRINGi79929.MTBMA_c15520.

Structurei

Secondary structure

1
443
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115Combined sources
Beta strandi17 – 237Combined sources
Helixi24 – 274Combined sources
Turni29 – 313Combined sources
Helixi33 – 4412Combined sources
Beta strandi45 – 495Combined sources
Helixi50 – 5910Combined sources
Helixi79 – 813Combined sources
Helixi82 – 9312Combined sources
Beta strandi102 – 1065Combined sources
Helixi107 – 1093Combined sources
Beta strandi111 – 1155Combined sources
Helixi118 – 1225Combined sources
Beta strandi125 – 1273Combined sources
Helixi129 – 14618Combined sources
Turni150 – 1523Combined sources
Helixi153 – 1619Combined sources
Turni162 – 1665Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi174 – 1763Combined sources
Helixi182 – 1843Combined sources
Helixi191 – 1933Combined sources
Helixi197 – 2037Combined sources
Turni204 – 2063Combined sources
Helixi208 – 22518Combined sources
Turni226 – 2294Combined sources
Helixi231 – 2333Combined sources
Helixi234 – 24512Combined sources
Helixi248 – 2503Combined sources
Helixi251 – 2599Combined sources
Turni260 – 2623Combined sources
Helixi265 – 27814Combined sources
Beta strandi283 – 2886Combined sources
Beta strandi291 – 2955Combined sources
Helixi299 – 32123Combined sources
Helixi324 – 3263Combined sources
Helixi327 – 34216Combined sources
Helixi347 – 3504Combined sources
Helixi351 – 36111Combined sources
Beta strandi364 – 3685Combined sources
Helixi372 – 3743Combined sources
Turni380 – 3823Combined sources
Beta strandi384 – 3896Combined sources
Helixi390 – 39910Combined sources
Helixi408 – 4114Combined sources
Helixi413 – 4197Combined sources
Helixi423 – 4264Combined sources
Helixi428 – 43912Combined sources
Turni440 – 4423Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MAKFEDKVDL YDDRGNLVEE QVPLEALSPL RNPAIKSIVQ GIKRTVAVNL
60 70 80 90 100
EGIENALKTA KVGGPACKIM GRELDLDIVG NAESIAAAAK EMIQVTEDDD
110 120 130 140 150
TNVELLGGGK RALVQVPSAR FDVAAEYSAA PLVTATAFVQ AIINEFDVSM
160 170 180 190 200
YDANMVKAAV LGRYPQSVEY MGANIATMLD IPQKLEGPGY ALRNIMVNHV
210 220 230 240 250
VAATLKNTLQ AAALSTILEQ TAMFEMGDAV GAFERMHLLG LAYQGMNADN
260 270 280 290 300
LVFDLVKANG KEGTVGSVIA DLVERALEDG VIKVEKELTD YKVYGTDDLA
310 320 330 340 350
MWNAYAAAGL MAATMVNQGA ARAAQGVSST LLYYNDLIEF ETGLPSVDFG
360 370 380 390 400
KVEGTAVGFS FFSHSIYGGG GPGIFNGNHI VTRHSKGFAI PCVAAAMALD
410 420 430 440
AGTQMFSPEA TSGLIKEVFS QVDEFREPLK YVVEAAAEIK NEI
Length:443
Mass (Da):47,240
Last modified:January 23, 2007 - v3
Checksum:i1237E83E405E6D6B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07794 Genomic DNA. Translation: CAA30635.1.
CP001710 Genomic DNA. Translation: ADL59131.1.
PIRiA28544.
RefSeqiWP_013296341.1. NC_014408.1.
YP_003850444.1. NC_014408.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07794 Genomic DNA. Translation: CAA30635.1.
CP001710 Genomic DNA. Translation: ADL59131.1.
PIRiA28544.
RefSeqiWP_013296341.1. NC_014408.1.
YP_003850444.1. NC_014408.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

STRINGi79929.MTBMA_c15520.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

HOGENOMiHOG000225842.
KOiK00401.
OMAiFREPLKY.

Enzyme and pathway databases

UniPathwayiUPA00646; UER00699.
BioCyciMMAR79929:GH5J-1556-MONOMER.
BRENDAi2.8.4.1. 7427.

Miscellaneous databases

EvolutionaryTraceiP11560.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 105 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.