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Reviewed, UniProtKB/Swiss-Prot P11559 (MCRA_METVO)

Last modified September 22, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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

Catalytic activity

2-(methylthio)ethanesulfonate (methyl-CoM) + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) = 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: EC

nickel 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
P11559-1 [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: 3185509] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 1537 / PS.

Cross-references

Sequence databases

X07793 Genomic DNA. Translation: CAA30633.1.
PIRS03261.

3D structure databases

HSSPHSSP built from PDB template 1E6V based on UniProtKB Q49605.
SMRP11559. Positions 6-553.
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.8.4.1. 20957.

Family and domain databases

InterProIPR016212. 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.
[Graphical view]
Gene3DG3DSA:1.20.840.10. MCR_a/b_chain_a-bundle. 1 hit.
G3DSA:3.90.390.10. Me_CoM_Rdtase_asu_N_sub1. 1 hit.
G3DSA:3.30.70.470. Me_CoM_Rdtase_asu_N_sub2. 1 hit.
PfamPF02249. MCR_alpha. 1 hit.
PF02745. MCR_alpha_N. 1 hit.
[Graphical view]
PIRSFPIRSF000262. MCR_alpha. 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: September 22, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents