P27355 (MEMG_METTR) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 69.
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: Methane monooxygenase component A gamma chain EC=1.14.13.25 Alternative name(s): Methane hydroxylase | ||
| Gene names |
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| Organism | Methylosinus trichosporium | ||
| Taxonomic identifier | 426 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Methylocystaceae › Methylosinus![]() |
Protein attributes
| Sequence length | 169 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Responsible for the initial oxygenation of methane to methanol in methanotrophs. It also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic and heterocyclic compounds. |
| Catalytic activity | Methane + NAD(P)H + O2 = methanol + NAD(P)+ + H2O. |
| Subunit structure | M.trichosporium has two forms of methane monooxygenase, a soluble and a membrane-bound type. The soluble type consists of four components (A to D): protein A, comprising three chains, in an alpha-2, beta-2, gamma-2 configuration, is a nonheme iron protein containing an unusual mu-hydroxo bridge structure at its active site and interacts with both oxygen and methane. |
Ontologies
| Keywords | |
|---|---|
| Biological process | One-carbon metabolism |
| Ligand | NADP |
| Molecular function | Monooxygenase Oxidoreductase |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | methane metabolic process Inferred from electronic annotation. Source: InterPro one-carbon metabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | methane monooxygenase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 | |||||||||||||||||||||||||||||
| Chain | 2 – 169 | 168 | Methane monooxygenase component A gamma chain | PRO_0000096410 | ||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||
| Beta strand | 7 – 9 | 3 | ||||||||||||||||||||||||||||||
| Helix | 11 – 21 | 11 | ||||||||||||||||||||||||||||||
| Helix | 26 – 40 | 15 | ||||||||||||||||||||||||||||||
| Turn | 49 – 53 | 5 | ||||||||||||||||||||||||||||||
| Helix | 54 – 72 | 19 | ||||||||||||||||||||||||||||||
| Helix | 75 – 80 | 6 | ||||||||||||||||||||||||||||||
| Helix | 88 – 100 | 13 | ||||||||||||||||||||||||||||||
| Helix | 105 – 119 | 15 | ||||||||||||||||||||||||||||||
| Turn | 120 – 123 | 4 | ||||||||||||||||||||||||||||||
| Helix | 126 – 144 | 19 | ||||||||||||||||||||||||||||||
| Turn | 145 – 149 | 5 | ||||||||||||||||||||||||||||||
| Helix | 153 – 160 | 8 | ||||||||||||||||||||||||||||||
| Beta strand | 163 – 167 | 5 | ||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Molecular analysis of the methane monooxygenase (MMO) gene cluster of Methylosinus trichosporium OB3b." Cardy D.L.N., Laidler V., Salmond G.P.C., Murrell J.C. Mol. Microbiol. 5:335-342(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: OB3b. |
| [2] | "Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification of sites of component interaction." Fox B.G., Liu Y., Dege J.E., Lipscomb J.D. J. Biol. Chem. 266:540-550(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-12. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | X55394 Genomic DNA. Translation: CAA39071.1. | ||||||||||||||||||
| PIR | C39049. S15210. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P27355. | ||||||||||||||||||
| SMR | P27355. Positions 2-168. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BioCyc | MetaCyc:MONOMER-3869. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| Gene3D | 1.20.1280.10. 1 hit. 1.20.1280.30. 1 hit. | ||||||||||||||||||
| InterPro | IPR004222. Me_mOase_g. IPR015952. Me_mOase_g_dom1. IPR015953. Me_mOase_g_dom2. [Graphical view] | ||||||||||||||||||
| Pfam | PF02964. MeMO_Hyd_G. 1 hit. [Graphical view] | ||||||||||||||||||
| PIRSF | PIRSF018503. Me_mOase_g. 1 hit. | ||||||||||||||||||
| ProDom | PD022203. Me_mOase_g. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||||||||
| SUPFAM | SSF47152. Me_mOase_hydro_g. 1 hit. | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| EvolutionaryTrace | P27355. | ||||||||||||||||||
Entry information
| Entry name | MEMG_METTR | ||||||||
| Accession | Primary (citable) accession number: P27355 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |

Clusters with
