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Q49605 (MCRA_METKA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 103. 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 I subunit alpha

Short name=MCR I alpha
EC=2.8.4.1
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase alpha
Gene names
Name:mcrA
Ordered Locus Names:MK0655
OrganismMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) [Reference proteome] [HAMAP]
Taxonomic identifier190192 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus

Protein attributes

Sequence length553 AA.
Sequence statusComplete.
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 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
   Technical term3D-structure
Complete 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 – 553553Methyl-coenzyme M reductase I subunit alpha
PRO_0000147454

Sites

Metal binding1501Nickel

Amino acid modifications

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

Experimental info

Sequence conflict901H → T in AAB02003. Ref.1
Sequence conflict3421T → P in AAB02003. Ref.1
Sequence conflict4411H → Q in AAB02003. Ref.1

Secondary structure

.......................................................................................... 553
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q49605 [UniParc].

Last modified April 16, 2002. Version 2.
Checksum: F26582E0DCF2A434

FASTA55361,384
        10         20         30         40         50         60 
MSSAEEKLFM KALKEKFEES PEEKYTKFYI FGGWKQSERK KEFKEWADKI VEERGVPHYN 

        70         80         90        100        110        120 
PDIGVPLGQR KLMSYQVSGT DVFVEGDDLH FVNNAAMQQM WDDIRRTVIV GMDTAHRVLE 

       130        140        150        160        170        180 
RRLGKEVTPE TINEYMETLN HALPGGAVVQ EHMVEIHPGL TWDCYAKIIT GDLELADEID 

       190        200        210        220        230        240 
DKFLIDIEKL FPEEQAEQLI KAIGNRTYQV CRMPTIVGHV CDGATMYRWA AMQIAMSFIC 

       250        260        270        280        290        300 
AYKIAAGEAA VSDFAFASKH AEVINMGEML PARRARGENE PGGVPFGVLA DCVQTMRKYP 

       310        320        330        340        350        360 
DDPAKVALEV IAAGAMLYDQ IWLGSYMSGG VGFTQYATAV YTDNILDDYV YYGLEYVEDK 

       370        380        390        400        410        420 
YGIAEAEPSM DVVKDVATEV TLYGLEQYER YPAAMETHFG GSQRAAVCAA AAGCSTAFAT 

       430        440        450        460        470        480 
GHAQAGLNGW YLSQILHKEG HGRLGFYGYA LQDQCGAANS LSVRSDEGLP LELRGPNYPN 

       490        500        510        520        530        540 
YAMNVGHLGE YAGIVQAAHA ARGDAFCVHP VIKVAFADEN LVFDFTEPRK EFAKGALREF 

       550 
EPAGERDLIV PAE 

« Hide

References

« Hide 'large scale' references
[1]"Phylogeny of Methanopyrus kandleri based on methyl coenzyme M reductase operons."
Noelling J., Elfner A., Palmer J.R., Steigerwald V.J., Pihl T.D., Lake J.A., Reeve J.N.
Int. J. Syst. Bacteriol. 46:1170-1173(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens."
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.
[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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U57340 Genomic DNA. Translation: AAB02003.1.
AE009439 Genomic DNA. Translation: AAM01870.1.
RefSeqNP_613940.1. NC_003551.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E6VX-ray2.70A/D1-553[»]
ProteinModelPortalQ49605.
SMRQ49605. Positions 8-552.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190192.MK0655.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM01870; AAM01870; MK0655.
GeneID1476756.
KEGGmka:MK0655.

Phylogenomic databases

eggNOGCOG4058.
HOGENOMHOG000225809.
KOK00399.
OMAAHSARGD.

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...

Other

EvolutionaryTraceQ49605.

Entry information

Entry nameMCRA_METKA
AccessionPrimary (citable) accession number: Q49605
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: April 16, 2002
Last modified: May 14, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways