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Protein

Methyl-coenzyme M reductase I subunit gamma

Gene

mcrG

Organism
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (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: methyl-coenzyme M reduction

This protein is involved in step 1 of the subpathway that synthesizes methane from methyl-coenzyme M.
Proteins known to be involved in this subpathway in this organism are:
  1. Methyl-coenzyme M reductase II subunit alpha (mrtA), Methyl-coenzyme M reductase II subunit gamma (mrtG), Methyl-coenzyme M reductase I subunit beta (mcrB), Methyl-coenzyme M reductase I subunit alpha (mcrA), Methyl-coenzyme M reductase I subunit gamma (mcrG)
This subpathway is part of the pathway methyl-coenzyme M reduction, which is itself part of One-carbon metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes methane from methyl-coenzyme M, the pathway methyl-coenzyme M reduction and in One-carbon metabolism.

GO - Molecular functioni

  • coenzyme-B sulfoethylthiotransferase activity Source: MENGO

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Methanogenesis

Enzyme and pathway databases

BRENDAi2.8.4.1. 7427.
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 ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri79929 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000000345 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001474792 – 249Methyl-coenzyme M reductase I subunit gammaAdd BLAST248

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

STRINGi79929.MTBMA_c15490.

Structurei

Secondary structure

1249
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 19Combined sources10
Helixi33 – 40Combined sources8
Beta strandi51 – 53Combined sources3
Helixi56 – 58Combined sources3
Helixi65 – 69Combined sources5
Helixi74 – 78Combined sources5
Beta strandi82 – 89Combined sources8
Turni91 – 93Combined sources3
Helixi98 – 108Combined sources11
Beta strandi113 – 116Combined sources4
Beta strandi121 – 126Combined sources6
Helixi127 – 139Combined sources13
Turni145 – 147Combined sources3
Beta strandi148 – 150Combined sources3
Beta strandi175 – 177Combined sources3
Turni179 – 181Combined sources3
Beta strandi184 – 188Combined sources5
Beta strandi194 – 200Combined sources7
Helixi207 – 213Combined sources7
Helixi224 – 226Combined sources3
Helixi228 – 247Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5A0YX-ray1.10C/F1-249[»]
5G0RX-ray1.25C/F1-249[»]
ProteinModelPortaliP11562.
SMRiP11562.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11562.

Family & Domainsi

Phylogenomic databases

eggNOGiarCOG04858. Archaea.
COG4057. LUCA.
HOGENOMiHOG000225820.
KOiK00402.
OMAiKRTTIYR.

Family and domain databases

CDDicd00539. MCR_gamma. 1 hit.
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.
RefSeqiWP_013296338.1. 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.
RefSeqiWP_013296338.1. NC_014408.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5A0YX-ray1.10C/F1-249[»]
5G0RX-ray1.25C/F1-249[»]
ProteinModelPortaliP11562.
SMRiP11562.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi79929.MTBMA_c15490.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiarCOG04858. Archaea.
COG4057. LUCA.
HOGENOMiHOG000225820.
KOiK00402.
OMAiKRTTIYR.

Enzyme and pathway databases

UniPathwayiUPA00646; UER00699.
BRENDAi2.8.4.1. 7427.

Miscellaneous databases

EvolutionaryTraceiP11562.

Family and domain databases

CDDicd00539. MCR_gamma. 1 hit.
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.
ProtoNetiSearch...

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 2, 2016
This is version 114 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

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 one 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.