Reviewed, UniProtKB/Swiss-Prot P11562 (MCRG_METTM)

Names and origin

Protein names

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

Gene names

Name:

mcrG

Organism

Methanobacterium thermoautotrophicum (strain Marburg / DSM 2133)

Taxonomic identifier

79929 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

Protein attributes

Sequence length	249 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.
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.
Developmental stage	There are two MCR complexes in this bacteria. MCR II is expressed in the early growth phase. Late growth cells contains mostly MCR I.

Ontologies

Keywords
Biological process	Methanogenesis
Molecular function	Transferase
Technical term	3D-structure Direct protein sequencing
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 Ref.2

Chain

2 – 249

248

Methyl-coenzyme M reductase I subunit gamma

PRO_0000147479

Secondary structure

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249

Helix Strand Turn

Details...

Helix

10 – 19

10

Helix

33 – 40

8

Beta strand

51 – 53

3

Helix

56 – 58

3

Helix

65 – 69

5

Helix

74 – 78

5

Beta strand

82 – 89

8

Turn

91 – 93

3

Helix

98 – 108

11

Beta strand

113 – 116

4

Beta strand

121 – 126

6

Helix

127 – 139

13

Turn

145 – 147

3

Beta strand

148 – 150

3

Beta strand

175 – 177

3

Turn

179 – 181

3

Beta strand

184 – 188

5

Beta strand

194 – 200

7

Helix

207 – 213

7

Helix

224 – 226

3

Helix

228 – 246

19

Sequences

	Sequence		Length	Mass (Da)
	P11562-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E39CD62AD7CCC6DC	FASTA	249	28,758
	10 20 30 40 50 60 MAQYYPGTTK VAQNRRNFCN PEYELEKLRE ISDEDVVKIL GHRAPGEEYP SVHPPLEEMD 70 80 90 100 110 120 EPEDAIREMV EPIDGAKAGD RVRYIQFTDS MYFAPAQPYV RSRAYLCRYR GADAGTLSGR 130 140 150 160 170 180 QIIETRERDL EKISKELLET EFFDPARSGV RGKSVHGHSL RLDEDGMMFD MLRRQIYNKD 190 200 210 220 230 240 TGRVEMVKNQ IGDELDEPVD LGEPLDEETL MEKTTIYRVD GEAYRDDVEA VEIMQRIHVL RSQGGFNLE

References

[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: 2448287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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: 2269306] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21.
[3]	"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: 9367957] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
[4]	"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: 11491299] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X07794 Genomic DNA. Translation: CAA30638.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR009024. Me_CoM_Rdtase_Fd-like_fold.
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. Me_CoM_Rdtase_gsu. 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_METTM

Accession

Primary (citable) accession number: P11562

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 72 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)