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P12972

- MCRB_METFE

UniProt

P12972 - MCRB_METFE

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Protein

Methyl-coenzyme M reductase subunit beta

Gene

mcrB

Organism
Methanothermus fervidus
Status
Reviewed - 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
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.

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:
EMBL
GenBank
DDBJ
Links Updated
J03375 Genomic DNA. Translation: AAA72193.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03375 Genomic DNA. Translation: AAA72193.1 .

3D structure databases

ProteinModelPortali P12972.
SMRi P12972. Positions 3-434.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00646 ; UER00699 .

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

  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: September 3, 2014
This is version 73 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