Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q60391 (MCRX_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase alpha
Gene names
Name:mrtA
Synonyms:mtrA
Ordered Locus Names:MJ0083
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length552 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 By similarity.

Ontologies

Keywords
   Biological processMethanogenesis
   LigandMetal-binding
Nickel
   Molecular functionTransferase
   PTMMethylation
   Technical termComplete proteome
Reference proteome
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 – 552552Methyl-coenzyme M reductase II subunit alpha
PRO_0000147453

Sites

Metal binding1501Nickel By similarity

Amino acid modifications

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

Sequences

Sequence LengthMass (Da)Tools
Q60391 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: DB66781796B987CE

FASTA55261,241
        10         20         30         40         50         60 
MDVEKKLFLK ALKEKFEEDP KEKYTKFYIF GGWRQSARKR EFVEFAQKLI EKRGGIPFYN 

        70         80         90        100        110        120 
PDIGVPLGQR KLMTYKISGT DAFVEGDDLH FCNNAAIQQL VDDIKRTVIV GMDTAHAVLE 

       130        140        150        160        170        180 
KRLGVEVTPE TINEYMETIN HALPGGAVVQ EHMVEVHPGL VWDCYAKIFT GNDELADEID 

       190        200        210        220        230        240 
KRFLIDINKE FPEEQAEQIK KYIGNRTYQV SRVPTIVVRC CDGGTVSRWS AMQIGMSFIT 

       250        260        270        280        290        300 
AYKLCAGEAA IADFSYAAKH ADVIQMGMIL PARRARGPNE PGGVPFGIFA DIIQTSRVSD 

       310        320        330        340        350        360 
DPAQVTLEVI GAAATFYDQV WLGSYMSGGV GFTQYASATY TDDILDDFVY YGMDYVEKKY 

       370        380        390        400        410        420 
GLCGVKPSME VVKDIATEVT LYGLEQYDEY PALLEDHFGG SQRAGVTAAA AGCSVAFATG 

       430        440        450        460        470        480 
NSNAGINGWY LSQILHKEYH SRLGFYGYDL QDQCGAANSL SIRSDEGLLH ECRGPNYPNY 

       490        500        510        520        530        540 
AMNVGHQPEY AGIAQAPHAA RGDAFCLNPI IKVAFADDNL IFDFKWPRKC IAKGALREFE 

       550 
PAGERDLIIP AA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB98063.1.
PIRC64310.
RefSeqNP_247047.1. NC_000909.1.

3D structure databases

ProteinModelPortalQ60391.
SMRQ60391. Positions 7-551.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243232.MJ0083.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB98063; AAB98063; MJ_0083.
GeneID1450922.
KEGGmja:MJ_0083.

Phylogenomic databases

eggNOGCOG4058.
KOK00399.
OMAGHQPEYA.
ProtClustDBCLSK876061.

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 nameMCRX_METJA
AccessionPrimary (citable) accession number: Q60391
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 16, 2013
This is version 94 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

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names