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P11562

- MCRG_METTM

UniProt

P11562 - MCRG_METTM

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Protein

Methyl-coenzyme M reductase I subunit gamma

Gene

mcrG

Organism
Methanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (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: MENGO

GO - Biological processi

  1. methanogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Methanogenesis

Enzyme and pathway databases

BioCyciMMAR79929:GH5J-1553-MONOMER.
UniPathwayiUPA00646; UER00699.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-coenzyme M reductase I subunit gamma (EC:2.8.4.1)
Short name:
MCR I gamma
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase gamma
Gene namesi
Name:mcrG
Ordered Locus Names:MTBMA_c15490
OrganismiMethanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri79929 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
ProteomesiUP000000345: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 249248Methyl-coenzyme M reductase I subunit gammaPRO_0000147479Add
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.

Structurei

Secondary structure

1
249
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 1910Combined sources
Helixi33 – 408Combined sources
Beta strandi51 – 533Combined sources
Helixi56 – 583Combined sources
Helixi65 – 695Combined sources
Helixi74 – 785Combined sources
Beta strandi82 – 898Combined sources
Turni91 – 933Combined sources
Helixi98 – 10811Combined sources
Beta strandi113 – 1164Combined sources
Beta strandi121 – 1266Combined sources
Helixi127 – 13913Combined sources
Turni145 – 1473Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi175 – 1773Combined sources
Turni179 – 1813Combined sources
Beta strandi184 – 1885Combined sources
Beta strandi194 – 2007Combined sources
Helixi207 – 2137Combined sources
Helixi224 – 2263Combined sources
Helixi228 – 24619Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HBMX-ray1.80C/F2-249[»]
1HBNX-ray1.16C/F2-249[»]
1HBOX-ray1.78C/F2-249[»]
1HBUX-ray1.90C/F2-249[»]
1MROX-ray1.16C/F2-248[»]
3M1VX-ray1.45C/F2-249[»]
3M2RX-ray1.30C/F2-249[»]
3M2UX-ray1.40C/F2-249[»]
3M2VX-ray1.80C/F2-249[»]
3M30X-ray1.45C/F2-249[»]
3M32X-ray1.35C/F2-249[»]
3POTX-ray1.20C/F1-249[»]
ProteinModelPortaliP11562.
SMRiP11562. Positions 2-248.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11562.

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000225820.
KOiK00402.
OMAiKRTTIYR.

Family and domain databases

Gene3Di3.90.320.20. 1 hit.
InterProiIPR009024. Me_CoM_Rdtase_Fd-like_fold.
IPR003178. Me_CoM_Rdtase_gsu.
[Graphical view]
PfamiPF02240. MCR_gamma. 1 hit.
[Graphical view]
PIRSFiPIRSF000264. Meth_CoM_rd_gama. 1 hit.
ProDomiPD005845. Me_CoM_Rdtase_gsu. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF55088. SSF55088. 1 hit.
TIGRFAMsiTIGR03259. met_CoM_red_gam. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11562-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAQYYPGTTK VAQNRRNFCN PEYELEKLRE ISDEDVVKIL GHRAPGEEYP
60 70 80 90 100
SVHPPLEEMD EPEDAIREMV EPIDGAKAGD RVRYIQFTDS MYFAPAQPYV
110 120 130 140 150
RSRAYLCRYR GADAGTLSGR QIIETRERDL EKISKELLET EFFDPARSGV
160 170 180 190 200
RGKSVHGHSL RLDEDGMMFD MLRRQIYNKD TGRVEMVKNQ IGDELDEPVD
210 220 230 240
LGEPLDEETL MEKTTIYRVD GEAYRDDVEA VEIMQRIHVL RSQGGFNLE
Length:249
Mass (Da):28,758
Last modified:January 23, 2007 - v3
Checksum:iE39CD62AD7CCC6DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07794 Genomic DNA. Translation: CAA30638.1.
CP001710 Genomic DNA. Translation: ADL59128.1.
RefSeqiYP_003850441.1. NC_014408.1.

Genome annotation databases

EnsemblBacteriaiADL59128; ADL59128; MTBMA_c15490.
GeneIDi9705258.
KEGGimmg:MTBMA_c15490.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07794 Genomic DNA. Translation: CAA30638.1 .
CP001710 Genomic DNA. Translation: ADL59128.1 .
RefSeqi YP_003850441.1. NC_014408.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HBM X-ray 1.80 C/F 2-249 [» ]
1HBN X-ray 1.16 C/F 2-249 [» ]
1HBO X-ray 1.78 C/F 2-249 [» ]
1HBU X-ray 1.90 C/F 2-249 [» ]
1MRO X-ray 1.16 C/F 2-248 [» ]
3M1V X-ray 1.45 C/F 2-249 [» ]
3M2R X-ray 1.30 C/F 2-249 [» ]
3M2U X-ray 1.40 C/F 2-249 [» ]
3M2V X-ray 1.80 C/F 2-249 [» ]
3M30 X-ray 1.45 C/F 2-249 [» ]
3M32 X-ray 1.35 C/F 2-249 [» ]
3POT X-ray 1.20 C/F 1-249 [» ]
ProteinModelPortali P11562.
SMRi P11562. Positions 2-248.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADL59128 ; ADL59128 ; MTBMA_c15490 .
GeneIDi 9705258.
KEGGi mmg:MTBMA_c15490.

Phylogenomic databases

HOGENOMi HOG000225820.
KOi K00402.
OMAi KRTTIYR.

Enzyme and pathway databases

UniPathwayi UPA00646 ; UER00699 .
BioCyci MMAR79929:GH5J-1553-MONOMER.

Miscellaneous databases

EvolutionaryTracei P11562.

Family and domain databases

Gene3Di 3.90.320.20. 1 hit.
InterProi IPR009024. Me_CoM_Rdtase_Fd-like_fold.
IPR003178. Me_CoM_Rdtase_gsu.
[Graphical view ]
Pfami PF02240. MCR_gamma. 1 hit.
[Graphical view ]
PIRSFi PIRSF000264. Meth_CoM_rd_gama. 1 hit.
ProDomi PD005845. Me_CoM_Rdtase_gsu. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF55088. SSF55088. 1 hit.
TIGRFAMsi TIGR03259. met_CoM_red_gam. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the methyl coenzyme M reductase genes from Methanobacterium thermoautotrophicum."
    Bokranz M., Baeumner G., Allmansberger R., Ankel-Fuchs D., Klein A.
    J. Bacteriol. 170:568-577(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
  2. "Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism."
    Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., Gottschalk G., Thauer R.K.
    J. Bacteriol. 192:5850-5851(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
  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: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
  4. "Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation."
    Ermler U., Grabarse W., Shima S., Goubeaud M., Thauer R.K.
    Science 278:1457-1462(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
  5. "On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding."
    Grabarse W., Mahlert F., Duin E.C., Goubeaud M., Shima S., Thauer R.K., Lamzin V., Ermler U.
    J. Mol. Biol. 309:315-330(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS).
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.

Entry informationi

Entry nameiMCRG_METTM
AccessioniPrimary (citable) accession number: P11562
Secondary accession number(s): D9PY30
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 101 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

3D-structure, Complete proteome, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3