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P12971 (MCRA_METFE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 76. 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
OrganismMethanothermus fervidus
Taxonomic identifier2180 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanothermaceaeMethanothermus

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_0000147450

Sites

Metal binding1501Nickel By similarity

Amino acid modifications

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

Sequences

Sequence LengthMass (Da)Tools
P12971 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: C2517AB56DA53D72

FASTA55561,550
        10         20         30         40         50         60 
MAEERKKLFV DALRKKFKEE PKERKTTFYT LGGWKQSERK KEFVEYGKKV AKERGIPAYN 

        70         80         90        100        110        120 
PDIGTPLGQR VLMPYQVSTT DTFVEGDDLH FVNNLAMQQF WDDIRRTVIV GLNHAHRILE 

       130        140        150        160        170        180 
RSLGKEVTPE TINHYLETVN HAMPGAAVVQ EHMVETHPGL TADSYVKVFT GNDELADEIE 

       190        200        210        220        230        240 
SCYLIDINKQ FPEHQAEQLK KAIGHTIWQA VRIPTIVSRT CDGATTSRWS AMQIGMSMIS 

       250        260        270        280        290        300 
AYKQAAGEAA TADFAYAAKH AEVIHLGTFL PVRRARGENE LGGVPFGFLA DIVQSSRVHY 

       310        320        330        340        350        360 
EDPVRVALDV VASGAMLYDQ IWLGSYMSGG VGFTQYATAS YTDNILDDFT YYGKEYVEDK 

       370        380        390        400        410        420 
YGGLAEAPHD FDTILDVATE VTLYSLDQYE EYPTLMEDHF GGSQRAAIAA AASGCSTAFA 

       430        440        450        460        470        480 
AGNAQAGLSG WYLSQILHKE CHARLGFYGY DLQDQCGAAN TYSIRSDEGL PAELRGPNYP 

       490        500        510        520        530        540 
NYAMNVGHLG EYAGIVQAAH IARGDADSLN PLVKVAFADD NLPFDWTNPR GEFAKGALRE 

       550 
FEPEGERDLI RPAGK 

« Hide

References

[1]"Structure and comparative analysis of the genes encoding component C of methyl coenzyme M reductase in the extremely thermophilic archaebacterium Methanothermus fervidus."
Weil C.F., Cram D.S., Sherf B.A., Reeve J.N.
J. Bacteriol. 170:4718-4726(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03375 Genomic DNA. Translation: AAA72197.1.

3D structure databases

ProteinModelPortalP12971.
SMRP12971. 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_METFE
AccessionPrimary (citable) accession number: P12971
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: October 16, 2013
This is version 76 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