Reviewed, UniProtKB/Swiss-Prot P21112 (MCRZ_METTH)

Names and origin

Protein names

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

Gene names

Name:	mrtG
Ordered Locus Names:	MTH_1130

Organism

Methanobacterium thermoautotrophicum [Complete proteome] [HAMAP]

Taxonomic identifier

187420 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

Protein attributes

Sequence length	265 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.
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	Complete proteome 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.3
	Chain	2 – 265	264	Methyl-coenzyme M reductase II subunit gamma		PRO_0000147480
Experimental info
	Sequence conflict	132	1	D → V in AAA73438. Ref.1
	Sequence conflict	230	1	D → DD in AAA73438. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P21112-1 [UniParc]. Last modified January 23, 2007. Version 5. Checksum: F1E6783AAE7A3CA8	FASTA	265	30,567
	10 20 30 40 50 60 MTYKAQYTPG ETQIAENRRK HMDPDYEFRK LREVSDEDLV KVLGHRNPGE SYKSVHPPLD 70 80 90 100 110 120 EMDFEEDIVR DMVEPIQGAK EGVRVRYIQF ADSMYNAPAQ PYDRARTYMW RYRGVDTGTL 130 140 150 160 170 180 SGRQVIEMRE LDLEGVSKEL VETELFDPAT TGIRGATVHG HSLRLDENGL MFDALQRYVF 190 200 210 220 230 240 DEEKGHVVYV KDQVGRPLDE PVDMGQPLGE DELKKITTIY RKDNIAMRDD KEAIEVVENI 250 260 HTGRTMGGFG MDVFKDDLRK RLGDD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7929010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Delta H.
[2]	"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics." Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N. J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Delta H.
[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: 2269306] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16. Strain: Delta H.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U09990 Genomic DNA. Translation: AAA73438.1. AE000666 Genomic DNA. Translation: AAB85619.1.
PIR	T45149.
RefSeq	NP_276258.1.
3D structure databases
HSSP	HSSP built from PDB template 1HBN based on UniProtKB P11562.
ModBase	Search...
Protein-protein interaction databases
STRING	P21112.
Genome annotation databases
GeneID	1471538.
GenomeReviews	Gene locus MTH_1130 in contig AE000666_GR.
KEGG	mth:MTH1130.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P21112.
Enzyme and pathway databases
BioCyc	MTHE187420:MTH1130-MON.
BRENDA	2.8.4.1. 270.
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

MCRZ_METTH

Accession

Primary (citable) accession number: P21112
Secondary accession number(s): O27202, Q50486

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	January 23, 2007
Last modified:	September 22, 2009
This is version 72 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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