Reviewed, UniProtKB/Swiss-Prot P07964 (MCRG_METBF)

Names and origin

Protein names

Recommended name:
    Methyl-coenzyme M reductase subunit gamma
    EC=2.8.4.1
Alternative name(s):
    Coenzyme-B sulfoethylthiotransferase gamma

Gene names

Name:	mcrG
Ordered Locus Names:	Mbar_A0894

Organism

Methanosarcina barkeri (strain Fusaro / DSM 804) [Complete proteome] [HAMAP]

Taxonomic identifier

269797 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and an heterodisulfide.
Catalytic activity	2-(methylthio)ethanesulfonate (methyl-CoM) + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) = CoM-S-S-CoB + methane.
Cofactor	Binds 2 coenzyme F430 noncovalently per hexamer. Coenzyme F430 is a yellow nickel porphinoid By similarity.
Pathway	One-carbon metabolism; methyl-coenzyme M reduction; methane from methyl-coenzyme M: step 1/1.
Subunit structure	Hexamer of two alpha, two beta, and two gamma chains.

Ontologies

Keywords
Biological process	Methanogenesis
Molecular function	Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	methanogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	coenzyme-B sulfoethylthiotransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 248

247

Methyl-coenzyme M reductase subunit gamma

PRO_0000147473

Secondary structure

1

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248

Helix Strand Turn

Details...

Helix

13 – 23

11

Helix

34 – 41

8

Beta strand

52 – 54

3

Helix

57 – 60

4

Helix

66 – 70

5

Helix

75 – 79

5

Beta strand

83 – 90

8

Turn

92 – 94

3

Helix

99 – 109

11

Beta strand

110 – 112

3

Beta strand

114 – 117

4

Beta strand

122 – 127

6

Helix

128 – 140

13

Turn

146 – 148

3

Beta strand

149 – 151

3

Beta strand

176 – 179

4

Beta strand

182 – 187

6

Beta strand

193 – 199

7

Helix

206 – 212

7

Helix

223 – 225

3

Helix

227 – 245

19

Sequences

	Sequence		Length	Mass (Da)
	P07964-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: AB23870B4BD7160B	FASTA	248	27,811
	10 20 30 40 50 60 MAYERQYYPG ATSVAANRRK HMSGKLEKLR EISDEDLTAV LGHRAPGSDY PSTHPPLAEM 70 80 90 100 110 120 GEPACSTREN VAATPGAAAG DRVRYIQFAD SMYNAPATPY FRSYFAAINF RGVDPGTLSG 130 140 150 160 170 180 RQIVEARERD MEQCAKVQME TEITDHALAG VRGATVHGHS VRLQEDGVMF DMLDRRRLEN 190 200 210 220 230 240 GTIIMDKDQV AIPLDRKVDL GKPMSSEEAA KRTTIYRVDN VAFRDDAEVV EWVHRIFDQR TKFGFQPK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the methyl coenzyme M reductase gene cluster from Methanosarcina barkeri." Bokranz M., Klein A. Nucleic Acids Res. 15:4350-4351(1987) [PubMed: 3502709] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes." Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R. J. Bacteriol. 188:7922-7931(2006) [PubMed: 16980466] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation." Grabarse W., Mahlert F., Shima S., Thauer R.K., Ermler U. J. Mol. Biol. 303:329-344(2000) [PubMed: 11023796] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

Y00158 Genomic DNA. Translation: CAA68356.1.
CP000099 Genomic DNA. Translation: AAZ69868.1.

PIR

D29525.

RefSeq

YP_304448.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E6Y	X-ray	1.60	C/F	2-248	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P07964.

Genome annotation databases

GeneID

3625939.

GenomeReviews

Gene locus Mbar_A0894 in contig CP000099_GR.

KEGG

mba:Mbar_A0894.

NMPDR

fig|269797.3.peg.414.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P07964.

OMA

GAKEGHR.

Enzyme and pathway databases

BioCyc

MBAR269797:MBAR_A0894-MON.

Family and domain databases

InterPro

IPR003178. Me_CoM_Rdtase_gsu.
[Graphical view]

Gene3D

G3DSA:3.90.320.20. MCR_gamma. 1 hit.

Pfam

PF02240. MCR_gamma. 1 hit.
[Graphical view]

PIRSF

PIRSF000264. Meth_CoM_rd_gama. 1 hit.

ProDom

PD005845. MCR_gamma. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR03259. met_CoM_red_gam. 1 hit.

ProtoNet

Search...

Entry information

Entry name

MCRG_METBF

Accession

Primary (citable) accession number: P07964
Secondary accession number(s): Q46E24

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 74 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)