Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Methyl-coenzyme M reductase subunit beta

Gene

mcrB

Organism
Methanothermus fervidus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein predictedi

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 subunit gamma (mcrG), Methyl-coenzyme M reductase subunit beta (mcrB), Methyl-coenzyme M reductase subunit alpha (mcrA)
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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Methanogenesis

Enzyme and pathway databases

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
OrganismiMethanothermus fervidus
Taxonomic identifieri2180 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanothermaceaeMethanothermus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 438438Methyl-coenzyme M reductase subunit betaPRO_0000147463Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi523846.Mfer_0788.

Structurei

3D structure databases

ProteinModelPortaliP12972.
SMRiP12972. Positions 3-434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

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.

P12972-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKYEDKVDL YDDRGNLVEE QVPIEALSPL RNTAIKKIIH DIKRTVAVNL
60 70 80 90 100
EGIENALRSA KVGGSGCHIP GRELDVDVID NAEAIAEKAK EMIQVEEGDD
110 120 130 140 150
TVVELLHDGK RALVKVPSSR LESAAEYSVA PLVTASAFIQ SIIDVCDISI
160 170 180 190 200
YDANMVKAAV LGRYPQSVEY VGGNIATMLD IPQKLEGPGY ALRNILVNHI
210 220 230 240 250
VAATLKNTLQ AVALSSILEH TAMFEMGDAV GKFERLHLLG LAYQGLNADN
260 270 280 290 300
LLYDLVKANG KDGTVGSVVE DVVERAKEDG VIKVEKELNG YKVYGTDDLA
310 320 330 340 350
LWNAYAAAGL VAATIVNQGA ARAAQGVSST ILYDNDIIEF ERGLPGVDFG
360 370 380 390 400
RAEGTAVGFS FFSHSIYGGG GPGIFNGNHI VTRHSKGFAI PCVAAAMALD
410 420 430
AGTQMFSPEL TSGLIKDVFS KVDEFREPLK YVVELQPK
Length:438
Mass (Da):47,034
Last modified:October 1, 1989 - v1
Checksum:i76E0EE0DCB8CEC75
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03375 Genomic DNA. Translation: AAA72193.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03375 Genomic DNA. Translation: AAA72193.1.

3D structure databases

ProteinModelPortaliP12972.
SMRiP12972. Positions 3-434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi523846.Mfer_0788.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00646; UER00699.

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

  1. "Structure and comparative analysis of the genes encoding component C of methyl coenzyme M reductase in the extremely thermophilic archaebacterium Methanothermus fervidus."
    Weil C.F., Cram D.S., Sherf B.A., Reeve J.N.
    J. Bacteriol. 170:4718-4726(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiMCRB_METFE
AccessioniPrimary (citable) accession number: P12972
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: June 24, 2015
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways

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.