Q58256 (MCRA_METJA) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 85.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended 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 |
| ||||
| Organism | Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) | ||||
| Taxonomic identifier | 243232 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus |
Protein attributes
| Sequence length | 553 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and an heterodisulfide By similarity. |
| 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 process | Methanogenesis |
| Ligand | Metal-binding Nickel |
| Molecular function | Transferase |
| PTM | Methylation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | methanogenesis Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | coenzyme-B sulfoethylthiotransferase activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 553 | 553 | Methyl-coenzyme M reductase I subunit alpha | PRO_0000147452 | |||||
Sites | |||||||||
| Metal binding | 150 | 1 | Nickel By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 260 | 1 | Pros-methylhistidine By similarity | ||||||
| Modified residue | 273 | 1 | 5-methylarginine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 424 | 1 | N → F in AAL29289. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. Venter J.C.Science 273:1058-1073(1996) [PubMed: 8688087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440. |
| [2] | "The mcrA gene as an alternative to 16S rRNA in the phylogenetic analysis of methanogen populations in landfill." Luton P.E., Wayne J.M., Sharp R.J., Riley P.W. Microbiology 148:3521-3530(2002) [PubMed: 12427943] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 340-478. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L77117 Genomic DNA. Translation: AAB98851.1. AF414040 Genomic DNA. Translation: AAL29289.1. |
| RefSeq | NP_247840.1. NC_000909.1. |
3D structure databases | |
| ProteinModelPortal | Q58256. |
| SMR | Q58256. Positions 7-552. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1451734. |
| GenomeReviews | Gene locus MJ0846 in contig L77117_GR. |
| KEGG | mja:MJ_0846. |
| NMPDR | fig|243232.1.peg.877. |
| TIGR | MJ0846. |
Phylogenomic databases | |
| HOGENOM | HBG541009. |
| OMA | TMDVVED. |
| ProtClustDB | CLSK876061. |
Enzyme and pathway databases | |
| BioCyc | MJAN243232:MJ_0846-MONOMER. |
Family and domain databases | |
| InterPro | IPR022681. 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] |
| Gene3D | G3DSA: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. |
| KO | K00399. |
| Pfam | PF02249. MCR_alpha. 1 hit. PF02745. MCR_alpha_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000262. MCR_alpha. 1 hit. |
| SUPFAM | SSF48081. MCR_alpha_beta_C. 1 hit. SSF55088. MCR_fer_like. 1 hit. |
| TIGRFAMs | TIGR03256. Met_CoM_red_alp. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | MCRA_METJA | ||||||||
| Accession | Primary (citable) accession number: Q58256 Secondary accession number(s): Q977G8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Methanococcus jannaschii Methanococcus jannaschii: entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |

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