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P11559 (MCRA_METVO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 77. 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 subunit alpha

EC=2.8.4.1
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase alpha
Gene names
Name:mcrA
OrganismMethanococcus voltae
Taxonomic identifier2188 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

Protein attributes

Sequence length555 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 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 processMethanogenesis
   LigandMetal-binding
Nickel
   Molecular functionTransferase
   PTMMethylation
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 – 555555Methyl-coenzyme M reductase subunit alpha
PRO_0000147461

Sites

Metal binding1521Nickel By similarity

Amino acid modifications

Modified residue2621Pros-methylhistidine By similarity
Modified residue27515-methylarginine By similarity

Sequences

Sequence LengthMass (Da)Tools
P11559 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: DCBCE5DC91EA69D5

FASTA55561,227
        10         20         30         40         50         60 
MEAEKRLFLK ALKEKFEEDP KEKFTKFYTY GGWQQSARKQ EFVSENEKIV AEKRGGIPMY 

        70         80         90        100        110        120 
NPDIGVPLGQ RKLMPYKISN TDTYVEGDDL HFMNNAAIQQ LWDDIRRTVI VGMDTAHMVL 

       130        140        150        160        170        180 
EKRLGVEVTP ETINEYMHTI NHSLPGGAAV VQEHMVEVHP SLAWDCYAKI FTGDDELADE 

       190        200        210        220        230        240 
LDDRFVIDIN KLFPEEQAEA SKAAIGKKTY QVSRVPSLVG RVCDGGTISR WSAMQIGMSF 

       250        260        270        280        290        300 
ITAYKLCAGE AAIADFSYAA KHADVIQMGN ALLGRRARGP NELGGVRFGI LSDVVQTTRV 

       310        320        330        340        350        360 
SDDPVEQSLE VVATGAALYD QIWLGSYMSG GVGFTQYATA SYTDDILDDF SYYGYEYVEK 

       370        380        390        400        410        420 
KYGRCGTKAT MDVVEDIASE VTLYALEQYD EYPALLEDHF GGSQRAAVAA AAAGISVCMA 

       430        440        450        460        470        480 
TGNSNAGVNG WYLSQILHKE YHSRLGFYGY DLQDQCGASN SLAIRNDEAS PLELRGPNYP 

       490        500        510        520        530        540 
NYAMNVGHQG EYAGIAQSAH SARGDAFATN ALIKVAFADP SLVFDFSKPR KEIARGALRE 

       550 
FEAAGERDPI LPAKI 

« Hide

References

[1]"Comparative analysis of genes encoding methyl coenzyme M reductase in methanogenic bacteria."
Klein A., Allmansberger R., Bokranz M., Knaub S., Mueller B., Muth E.
Mol. Gen. Genet. 213:409-420(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07793 Genomic DNA. Translation: CAA30633.1.
PIRS03261.

3D structure databases

ProteinModelPortalP11559.
SMRP11559. Positions 7-553.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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 nameMCRA_METVO
AccessionPrimary (citable) accession number: P11559
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: October 16, 2013
This is version 77 of the entry and version 1 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