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Protein

Methyl-coenzyme M reductase I subunit beta

Gene

mcrB

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (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.

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

BioCyciMetaCyc:MCRBMAUTO-MONOMER.
MTHE187420:GJNM-1170-MONOMER.
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:MTH_1168
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
ProteomesiUP000005223 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 443442Methyl-coenzyme M reductase I subunit betaPRO_0000147467Add
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

IntActiO27236. 1 interaction.
STRINGi187420.MTH1168.

Structurei

3D structure databases

ProteinModelPortaliO27236.
SMRiO27236. Positions 2-443.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiCOG4054.
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.

O27236-1 [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
TKVELLGGGK 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 ETGLPGVDFG
360 370 380 390 400
KVEGTAVGFS FFSHSIYGGG GPGIFNGNHI VTRHSKGFAI PCVAAAMALD
410 420 430 440
AGTQMFSPEA TSGLIKEVFS QVDEFREPLK YVVEAAAEIK NEI
Length:443
Mass (Da):47,224
Last modified:January 23, 2007 - v3
Checksum:i132DFCD54BBB734E
GO

Sequence cautioni

The sequence AAB85657.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821A → C in AAA73441 (PubMed:7929010).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10036 Genomic DNA. Translation: AAA73441.1.
AE000666 Genomic DNA. Translation: AAB85657.1. Different initiation.
PIRiF69022.
RefSeqiNP_276296.1. NC_000916.1.

Genome annotation databases

EnsemblBacteriaiAAB85657; AAB85657; MTH_1168.
GeneIDi1471576.
KEGGimth:MTH1168.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10036 Genomic DNA. Translation: AAA73441.1.
AE000666 Genomic DNA. Translation: AAB85657.1. Different initiation.
PIRiF69022.
RefSeqiNP_276296.1. NC_000916.1.

3D structure databases

ProteinModelPortaliO27236.
SMRiO27236. Positions 2-443.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO27236. 1 interaction.
STRINGi187420.MTH1168.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB85657; AAB85657; MTH_1168.
GeneIDi1471576.
KEGGimth:MTH1168.

Phylogenomic databases

eggNOGiCOG4054.
KOiK00401.
OMAiFREPLKY.

Enzyme and pathway databases

UniPathwayiUPA00646; UER00699.
BioCyciMetaCyc:MCRBMAUTO-MONOMER.
MTHE187420:GJNM-1170-MONOMER.

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. "Growth phase-dependent transcription of the genes that encode the two methyl coenzyme M reductase isoenzymes and N5-methyltetrahydromethanopterin:coenzyme M methyltransferase in Methanobacterium thermoautotrophicum delta H."
    Pihl T.D., Sharma S., Reeve J.N.
    J. Bacteriol. 176:6384-6391(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
  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: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Entry informationi

Entry nameiMCRB_METTH
AccessioniPrimary (citable) accession number: O27236
Secondary accession number(s): Q50489
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: January 7, 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

Complete proteome, Direct protein sequencing, Reference proteome

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.