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P58815 (MCRX_METTM) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methyl-coenzyme M reductase II subunit alpha

Short name=MCR II alpha
EC=2.8.4.1
Gene names
Name:mrtA
Ordered Locus Names:MTBMA_c15120
OrganismMethanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) [Complete proteome] [HAMAP]
Taxonomic identifier79929 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length553 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and a heterodisulfide.

Catalytic activity

Methyl-CoM + CoB = 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 processMethanogenesis
   LigandMetal-binding
Nickel
   Molecular functionTransferase
   PTMMethylation
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processmethanogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncoenzyme-B sulfoethylthiotransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 553553Methyl-coenzyme M reductase II subunit alpha
PRO_0000147458

Sites

Metal binding1501Nickel By similarity

Amino acid modifications

Modified residue2601Pros-methylhistidine By similarity
Modified residue27315-methylarginine By similarity

Experimental info

Sequence conflict21D → L AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P58815 [UniParc].

Last modified November 30, 2010. Version 2.
Checksum: 94CC0D641E7C8271

FASTA55360,678
        10         20         30         40         50         60 
MDEKKLFLKA LKKKFEGEDP DEKYTNFYCF GGWEQSARKK EFTEYAKKAA EKRGGIPFYN 

        70         80         90        100        110        120 
PDIGVPLGQR KLMAYRVSGT DAYVEGDDLH FVNNAAIQQM VDDIKRTVIV GMDTAHAVLE 

       130        140        150        160        170        180 
KRLGVEVTPE TINEYMEAIN HALPGGAVVQ EHMVEVHPGL VEDCYAKIFT GDDNLADELD 

       190        200        210        220        230        240 
KRILIDINKE FPEEQAEQLK SYIGNRTYQV NRVPTIVVRT CDGGTVSRWS AMQIGMSFIS 

       250        260        270        280        290        300 
AYKLCAGEAA IADFSYAAKH ADVIEMGTIM PARRARGPNE PGGVAFGTFA DIVQTSRVSD 

       310        320        330        340        350        360 
DPANVSLEVI AGAAALYDQV WLGSYMSGGV GFTQYATAAY TDDILDDFVY YGMEYVDDKY 

       370        380        390        400        410        420 
GICGTKPTMD VVRDISTEVT LYSLEQYEEY PTLLEDHFGG SQRAAVAAAA AGCSTAFATG 

       430        440        450        460        470        480 
NSNAGINGWY LSQILHKEAH SRLGFYGYDL QDQCGASNSL SIRSDEGLIH ELRGPNYPNY 

       490        500        510        520        530        540 
AMNVGHQPEY AGIAQAPHAA RGDAFCTNPL IKVAFADKDL AFDFTSPRKS IAAGALREFM 

       550 
PEGERDLIIP AGK 

« Hide

References

« Hide 'large scale' references
[1]"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.
[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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-14.
Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001710 Genomic DNA. Translation: ADL59091.1.
RefSeqYP_003850404.1. NC_014408.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADL59091; ADL59091; MTBMA_c15120.
GeneID9705221.
KEGGmmg:MTBMA_c15120.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000225809.
KOK00399.
OMAGHQPEYA.

Enzyme and pathway databases

BioCycMMAR79929:GH5J-1516-MONOMER.
UniPathwayUPA00646; UER00699.

Family and domain databases

Gene3D1.20.840.10. 1 hit.
3.30.70.470. 1 hit.
3.90.390.10. 1 hit.
InterProIPR022681. MCR_a/b_chain_a-bundle.
IPR016212. Me_CoM_Rdtase_asu.
IPR008924. Me_CoM_Rdtase_asu/bsu_C.
IPR009047. Me_CoM_Rdtase_asu_C.
IPR003183. Me_CoM_Rdtase_asu_N.
IPR015811. Me_CoM_Rdtase_asu_N_sub1.
IPR015823. Me_CoM_Rdtase_asu_N_sub2.
IPR009024. Me_CoM_Rdtase_Fd-like_fold.
[Graphical view]
PfamPF02249. MCR_alpha. 1 hit.
PF02745. MCR_alpha_N. 1 hit.
[Graphical view]
PIRSFPIRSF000262. MCR_alpha. 1 hit.
SUPFAMSSF48081. SSF48081. 1 hit.
SSF55088. SSF55088. 1 hit.
TIGRFAMsTIGR03256. met_CoM_red_alp. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMCRX_METTM
AccessionPrimary (citable) accession number: P58815
Secondary accession number(s): D9PXZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: November 30, 2010
Last modified: October 16, 2013
This is version 48 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways