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P07961 (MCRA_METVA) 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 vannielii
Taxonomic identifier2187 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

Protein attributes

Sequence length553 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 – 553553Methyl-coenzyme M reductase subunit alpha
PRO_0000147460

Sites

Metal binding1511Nickel By similarity

Amino acid modifications

Modified residue2611Pros-methylhistidine By similarity
Modified residue27415-methylarginine By similarity

Sequences

Sequence LengthMass (Da)Tools
P07961 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 7B91F2DDA4B98489

FASTA55360,838
        10         20         30         40         50         60 
MEAEKRLFLK ALKEKFEEDP KEKYTKFYTY GGWEQSVRKR EFVAANEKVL AEKRQGVPLY 

        70         80         90        100        110        120 
NPDIGVPLGQ RKLMPYKLSG TDSYCEGDDL HFMNNAAIQQ LWDDIRRTVV VGMDTAHSVL 

       130        140        150        160        170        180 
EKRLGVEVTP ETINEYMHTI NHALSGGAVV QEHMVEVHPS LAWDSYARIF TGDDELAAEL 

       190        200        210        220        230        240 
DSRFLIDINK LFPAEQAEAL KKAIGKKTYQ VSRVPSLVGR VCDGGTISRW SAMQIGMSFI 

       250        260        270        280        290        300 
TAYKLCAGEA ATADFSYASK HADVIQMGNA LPGRRARGPN EPGGIQFGIL SDVVQTTRVS 

       310        320        330        340        350        360 
DDPVEQSLEV VAAGAALYDQ IWLGAYMSGG VGFTQYATAA YTDDILDDFS YYALDYVEKK 

       370        380        390        400        410        420 
YGRMGTKATM DVVEDIASEV TLYSLEQYDE YPALLEDHFG GSQRAAVAAA ASGIGVCMAT 

       430        440        450        460        470        480 
GNSNAGVNGW YLSQILHKEY HSRLGFYGYD LQDQCGASNS LAIRNDESAP LELRGPNYPN 

       490        500        510        520        530        540 
YAMNVGHQGE YAGIAQAAHS ARGDAFAMSA LIKVAFADPM LVFDFSKPRK EFARGALREF 

       550 
DAAGERDVIL PAK 

« Hide

References

[1]"Structure and expression of the genes, mcrBDCGA, which encode the subunits of component C of methyl coenzyme M reductase in Methanococcus vannielii."
Cram D.S., Sherf B.A., Libby R.T., Mattaliano R.J., Ramachandran K.L., Reeve J.N.
Proc. Natl. Acad. Sci. U.S.A. 84:3992-3996(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16893 Genomic DNA. Translation: AAA72598.1.
PIRE27793.

3D structure databases

ProteinModelPortalP07961.
SMRP07961. Positions 7-552.
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_METVA
AccessionPrimary (citable) accession number: P07961
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
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