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P21111

- MCRY_METTH

UniProt

P21111 - MCRY_METTH

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Protein

Methyl-coenzyme M reductase II subunit beta

Gene

mrtB

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed - 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:MRTBMAUTO-MONOMER.
MTHE187420:GJNM-1134-MONOMER.
UniPathwayiUPA00646; UER00699.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-coenzyme M reductase II subunit beta (EC:2.8.4.1)
Short name:
MCR II beta
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase beta
Gene namesi
Name:mrtB
Ordered Locus Names:MTH_1132
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
ProteomesiUP000005223: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 443442Methyl-coenzyme M reductase II subunit betaPRO_0000147469Add
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

IntActiP21111. 1 interaction.
STRINGi187420.MTH1132.

Structurei

3D structure databases

ProteinModelPortaliP21111.
SMRiP21111. Positions 4-443.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiCOG4054.
KOiK00401.
OMAiWALWNAY.

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.

P21111-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPMYEDRIDL YGADGKLLEE DVPLEAVSPL KNPTIANLVS DVKRSVAVNL
60 70 80 90 100
AGIEGSLKKA ALGGKSNFIP GREVELPIVE NAEAIAEKVK RLVQTSEDDD
110 120 130 140 150
TNIRLINNGQ QILVQVPTTR MGVAADYTVS ALVTGAAVVQ AIIDEFDVDM
160 170 180 190 200
FDANAVKTAV MGRYPQTVDF TGANLSTLLG PPVLLEGLGY GLRNIMANHV
210 220 230 240 250
VAITRKNTLN ASALSSILEQ TAMFETGDAV GAFERMHLLG LAYQGLNANN
260 270 280 290 300
LLFDLVKENS KGTVGTVIAS LVERAIEDRV IKVASEMKSG YKMYEPADWA
310 320 330 340 350
LWNAYAATGL LAATIVNVGA ARAAQGVAST VLYYNDILEY ETGLPGVDFG
360 370 380 390 400
RAMGTAVGFS FFSHSIYGGG GPGIFHGNHV VTRHSKGFAL PCVAAAMCLD
410 420 430 440
AGTQMFSVEK TSGLIGSVYS EIDYFREPIV NVAKGAAEIK DQL
Length:443
Mass (Da):47,134
Last modified:January 23, 2007 - v4
Checksum:i462293DE946E994E
GO

Sequence cautioni

The sequence AAB85621.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti294 – 2941Y → I in AAA73436. (PubMed:7929010)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09990 Genomic DNA. Translation: AAA73436.1.
AE000666 Genomic DNA. Translation: AAB85621.1. Different initiation.
J04540 Genomic DNA. Translation: AAB02353.1.
PIRiG69017.
T45147.
RefSeqiNP_276260.1. NC_000916.1.

Genome annotation databases

EnsemblBacteriaiAAB85621; AAB85621; MTH_1132.
GeneIDi1471540.
KEGGimth:MTH1132.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09990 Genomic DNA. Translation: AAA73436.1 .
AE000666 Genomic DNA. Translation: AAB85621.1 . Different initiation.
J04540 Genomic DNA. Translation: AAB02353.1 .
PIRi G69017.
T45147.
RefSeqi NP_276260.1. NC_000916.1.

3D structure databases

ProteinModelPortali P21111.
SMRi P21111. Positions 4-443.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P21111. 1 interaction.
STRINGi 187420.MTH1132.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB85621 ; AAB85621 ; MTH_1132 .
GeneIDi 1471540.
KEGGi mth:MTH1132.

Phylogenomic databases

eggNOGi COG4054.
KOi K00401.
OMAi WALWNAY.

Enzyme and pathway databases

UniPathwayi UPA00646 ; UER00699 .
BioCyci MetaCyc:MRTBMAUTO-MONOMER.
MTHE187420:GJNM-1134-MONOMER.

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

« 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. "A hydrogenase-linked gene in Methanobacterium thermoautotrophicum strain delta H encodes a polyferredoxin."
    Reeve J.N., Beckler G.S., Cram D.S., Hamilton P.T., Brown J.W., Krzycki J.A., Kolodziej A.F., Alex L., Orme-Johnson W.H., Walsh C.T.
    Proc. Natl. Acad. Sci. U.S.A. 86:3031-3035(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-146.
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
  4. "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 2-20.
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Entry informationi

Entry nameiMCRY_METTH
AccessioniPrimary (citable) accession number: P21111
Secondary accession number(s): O27204
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: October 1, 2014
This is version 103 of the entry and version 4 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