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Reviewed, UniProtKB/Swiss-Prot P11558 (MCRA_METTM)

Last modified February 9, 2010. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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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
OrganismMethanobacterium thermoautotrophicum (strain Marburg / DSM 2133)
Taxonomic identifier79929 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

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Protein attributes

Sequence length550 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

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.

Developmental stage

There are two MCR complexes in this bacteria. MCR II is expressed in the early growth phase. Late growth cells contains mostly MCR I.

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Ontologies

Keywords
   Biological processMethanogenesis
   LigandMetal-binding
Nickel
   Molecular functionTransferase
   PTMMethylation
   Technical term3D-structure
Direct protein sequencing
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 550549Methyl-coenzyme M reductase I subunit alpha
PRO_0000147456

Sites

Metal binding1471Nickel

Amino acid modifications

Modified residue2571Pros-methylhistidine
Modified residue27115-methylarginine
Modified residue40012-methylglutamine
Modified residue44511-thioglycine
Modified residue4521S-methylcysteine

Secondary structure

1 ......................................................................................... 550
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P11558-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D55A724B6CA9EFEE

FASTA55060,511
        10         20         30         40         50         60 
MADKLFINAL KKKFEESPEE KKTTFYTLGG WKQSERKTEF VNAGKEVAAK RGIPQYNPDI 

        70         80         90        100        110        120 
GTPLGQRVLM PYQVSTTDTY VEGDDLHFVN NAAMQQMWDD IRRTVIVGLN HAHAVIEKRL 

       130        140        150        160        170        180 
GKEVTPETIT HYLETVNHAM PGAAVVQEHM VETHPALVAD SYVKVFTGND EIADEIDPAF 

       190        200        210        220        230        240 
VIDINKQFPE DQAETLKAEV GDGIWQVVRI PTIVSRTCDG ATTSRWSAMQ IGMSMISAYK 

       250        260        270        280        290        300 
QAAGEAATGD FAYAAKHAEV IHMGTYLPVR RARGENEPGG VPFGYLADIC QSSRVNYEDP 

       310        320        330        340        350        360 
VRVSLDVVAT GAMLYDQIWL GSYMSGGVGF TQYATAAYTD NILDDFTYFG KEYVEDKYGL 

       370        380        390        400        410        420 
CEAPNNMDTV LDVATEVTFY GLEQYEEYPA LLEDQFGGSQ RAAVVAAAAG CSTAFATGNA 

       430        440        450        460        470        480 
QTGLSGWYLS MYLHKEQHSR LGFYGYDLQD QCGASNVFSI RGDEGLPLEL RGPNYPNYAM 

       490        500        510        520        530        540 
NVGHQGEYAG ISQAPHAARG DAFVFNPLVK IAFADDNLVF DFTNVRGEFA KGALREFEPA 

       550 
GERALITPAK

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References

[1]"Cloning and characterization of the methyl coenzyme M reductase genes from Methanobacterium thermoautotrophicum."
Bokranz M., Baeumner G., Allmansberger R., Ankel-Fuchs D., Klein A.
J. Bacteriol. 170:568-577(1988) [PubMed: 2448287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Two genetically distinct methyl-coenzyme M reductases in Methanobacterium thermoautotrophicum strain Marburg and delta H."
Rospert S., Linder D., Ellermann J., Thauer R.K.
Eur. J. Biochem. 194:871-877(1990) [PubMed: 2269306] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-19.
[3]"The biosynthesis of methylated amino acids in the active site region of methyl-coenzyme M reductase."
Selmer T., Kahnt J., Goubeaud M., Shima S., Grabarse W., Ermler U., Thauer R.K.
J. Biol. Chem. 275:3755-3760(2000) [PubMed: 10660523] [Abstract]
Cited for: POST-TRANSLATIONAL MODIFICATIONS.
[4]"Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation."
Ermler U., Grabarse W., Shima S., Goubeaud M., Thauer R.K.
Science 278:1457-1462(1997) [PubMed: 9367957] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
[5]"On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding."
Grabarse W., Mahlert F., Duin E.C., Goubeaud M., Shima S., Thauer R.K., Lamzin V., Ermler U.
J. Mol. Biol. 309:315-330(2001) [PubMed: 11491299] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS).

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X07794 Genomic DNA. Translation: CAA30639.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HBMX-ray1.80A/D2-550[»]
1HBNX-ray1.16A/D2-550[»]
1HBOX-ray1.78A/D2-550[»]
1HBUX-ray1.90A/D2-550[»]
1MROX-ray1.16A/D2-549[»]
ModBaseSearch...

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.
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.
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...

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Entry information

Entry nameMCRA_METTM
AccessionPrimary (citable) accession number: P11558
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: February 9, 2010
This is version 77 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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