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P07962 (MCRA_METBF) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Ordered Locus Names:Mbar_A0893
OrganismMethanosarcina barkeri (strain Fusaro / DSM 804) [Complete proteome] [HAMAP]
Taxonomic identifier269797 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length570 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and an 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
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processmethanogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncoenzyme-B sulfoethylthiotransferase activity

Inferred from electronic annotation. Source: 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

Initiator methionine11Removed
Chain2 – 570569Methyl-coenzyme M reductase subunit alpha
PRO_0000147449

Sites

Metal binding1611Nickel

Amino acid modifications

Modified residue2711Pros-methylhistidine
Modified residue28515-methylarginine
Modified residue46511-thioglycine
Modified residue4721S-methylcysteine

Secondary structure

1 .............................................................................................. 570
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07962 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 301E10CE7D449C76

FASTA57061,962
        10         20         30         40         50         60 
MAADIFSKFK KDMEVKFAQE FGSNKQTGGD ITDKTAKFLR LGPEQDPRKV EMIKAGKEIA 

        70         80         90        100        110        120 
EKRGIAFYNP MMHSGAPLGQ RAITPYTISG TDIVCEPDDL HYVNNAAMQQ MWDDIRRTCI 

       130        140        150        160        170        180 
VGLDMAHETL EKRLGKEVTP ETINHYLEVL NHAMPGAAVV QEMMVETHPA LVDDCYVKVF 

       190        200        210        220        230        240 
TGDDALADEI DKQFLIDINK EFSEEQAAQI KASIGKTSWQ AIHIPTIVSR TTDGAQTSRW 

       250        260        270        280        290        300 
AAMQIGMSFI SAYAMCAGEA AVADLSFAAK HAALVSMGEM LPARRARGPN EPGGLSFGHL 

       310        320        330        340        350        360 
SDIVQTSRVS EDPAKIALEV VGAGCMLYDQ IWLGSYMSGG VGFTQYATAA YTDDILDNNT 

       370        380        390        400        410        420 
YYDVDYINDK YNGAATVGKD NKVKASLEVV KDIATESTLY GIETYEKFPT ALEDHFGGSQ 

       430        440        450        460        470        480 
RATVLAAAAG VACSLATGNA NAGLSGWYLS MYLHKEAWGR LGFFGFDLQD QCGATNVLSY 

       490        500        510        520        530        540 
QGDEGLPDEL RGPNYPNYAM NVGHQGGYAG IAQAAHSGRG DAFTVNPLLK VCFADDLLPF 

       550        560        570 
NFAEPRREFG RGAIREFVPA GERSLVIPAK

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the methyl coenzyme M reductase gene cluster from Methanosarcina barkeri."
Bokranz M., Klein A.
Nucleic Acids Res. 15:4350-4351(1987) [PubMed: 3502709] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes."
Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.
J. Bacteriol. 188:7922-7931(2006) [PubMed: 16980466] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Fusaro / DSM 804.
[3]"Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation."
Grabarse W., Mahlert F., Shima S., Thauer R.K., Ermler U.
J. Mol. Biol. 303:329-344(2000) [PubMed: 11023796] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y00158 Genomic DNA. Translation: CAA68357.1.
CP000099 Genomic DNA. Translation: AAZ69867.1.
PIRE29525.
RefSeqYP_304447.1. NC_007355.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E6YX-ray1.60A/D2-570[»]
ProteinModelPortalP07962.
SMRP07962. Positions 2-569.
ModBaseSearch...

Protein-protein interaction databases

STRINGP07962.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3625938.
GenomeReviewsGene locus Mbar_A0893 in contig CP000099_GR.
KEGGmba:Mbar_A0893.
NMPDRfig|269797.3.peg.413.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04802.
HOGENOMHBG541009.
OMAQPEYAGI.
ProtClustDBCLSK876061.

Enzyme and pathway databases

BioCycMBAR269797:MBAR_A0893-MONOMER.

Family and domain databases

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]
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.
KOK00399.
PfamPF02249. MCR_alpha. 1 hit.
PF02745. MCR_alpha_N. 1 hit.
[Graphical view]
PIRSFPIRSF000262. MCR_alpha. 1 hit.
SUPFAMSSF48081. MCR_alpha_beta_C. 1 hit.
SSF55088. MCR_fer_like. 1 hit.
TIGRFAMsTIGR03256. Met_CoM_red_alp. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMCRA_METBF
AccessionPrimary (citable) accession number: P07962
Secondary accession number(s): Q46E25
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 97 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents