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Protein

Methyl-coenzyme M reductase subunit beta

Gene

mcrB

Organism
Methanococcus voltae
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.

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

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
OrganismiMethanococcus voltae
Taxonomic identifieri2188 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443Methyl-coenzyme M reductase subunit betaPRO_0000147472Add
BLAST

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP11561.
SMRiP11561. Positions 3-443.
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.

P11561-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVKYEDKICL FDAKGNQVAE DVPLEAISPL NNPTIMGMVK NIKRTVAVNL
60 70 80 90 100
AGIEESLAKG KIGGKGCQVP GTNIELDVIG DAEAIADKVK SILQVSAGDD
110 120 130 140 150
TEVKLINGGK QMAEQVPSKR LDVAAEYSVS MLSTGMALKE ALITNFNIDM
160 170 180 190 200
FDGSTVHSAI MGQYPQDMDY AGGNIASLLG APSKLEGLGY ALRNIPVNHA
210 220 230 240 250
VATTKKSLMN AIAFSSILEQ TAMFEMGDAV GSFERQHLLG LAYQGLNADN
260 270 280 290 300
LVVELVKANA TGTVGSVVNS IVEKAIADGV IVVDKTLGSG FNMYKPADVN
310 320 330 340 350
KWNAYAAAGL VAAVMVSCGA ARAAQNVAST ILYYNDILEY ETGLPGVDYG
360 370 380 390 400
RSMGTAVGFS FFSHSIYGGG GPGIFNGNHV VTRHSKGFAI PPVCAAMCMD
410 420 430 440
AGTQMFSPEK TSALVGTVYS AFDEFREPLK YVIEGALEVQ NKL
Length:443
Mass (Da):46,681
Last modified:October 1, 1989 - v1
Checksum:iE9E545ED9E48AB3F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07793 Genomic DNA. Translation: CAA30630.1.
PIRiS03257.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07793 Genomic DNA. Translation: CAA30630.1.
PIRiS03257.

3D structure databases

ProteinModelPortaliP11561.
SMRiP11561. Positions 3-443.
ModBaseiSearch...
MobiDBiSearch...

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. "Comparative analysis of genes encoding methyl coenzyme M reductase in methanogenic bacteria."
    Klein A., Allmansberger R., Bokranz M., Knaub S., Mueller B., Muth E.
    Mol. Gen. Genet. 213:409-420(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS.

Entry informationi

Entry nameiMCRB_METVO
AccessioniPrimary (citable) accession number: P11561
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: September 3, 2014
This is version 72 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.