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P27354

- MEMB_METTR

UniProt

P27354 - MEMB_METTR

Protein

Methane monooxygenase component A beta chain

Gene

mmoY

Organism
Methylosinus trichosporium
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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 activityi

    Methane + NAD(P)H + O2 = methanol + NAD(P)+ + H2O.

    GO - Molecular functioni

    1. methane monooxygenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular aromatic compound metabolic process Source: InterPro
    2. one-carbon metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-3868.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methane monooxygenase component A beta chain (EC:1.14.13.25)
    Alternative name(s):
    Methane hydroxylase
    Gene namesi
    Name:mmoY
    OrganismiMethylosinus trichosporium
    Taxonomic identifieri426 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylocystaceaeMethylosinus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 394393Methane monooxygenase component A beta chainPRO_0000096408Add
    BLAST

    Interactioni

    Subunit structurei

    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.

    Structurei

    Secondary structure

    1
    394
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni13 – 153
    Helixi17 – 2610
    Turni38 – 414
    Beta strandi45 – 484
    Helixi51 – 566
    Helixi88 – 903
    Helixi98 – 1003
    Helixi109 – 13325
    Helixi135 – 1384
    Helixi141 – 1455
    Helixi148 – 17225
    Helixi176 – 20631
    Helixi215 – 2239
    Helixi225 – 2273
    Helixi228 – 23912
    Helixi244 – 25310
    Helixi255 – 26410
    Turni265 – 2673
    Helixi268 – 2725
    Turni273 – 2764
    Helixi280 – 30223
    Helixi303 – 3075
    Turni310 – 3123
    Helixi313 – 33826
    Helixi339 – 3446
    Helixi364 – 3685
    Helixi373 – 3753
    Helixi381 – 3899

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MHYX-ray2.00B1-394[»]
    1MHZX-ray2.70B1-394[»]
    ProteinModelPortaliP27354.
    SMRiP27354. Positions 11-392.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27354.

    Family & Domainsi

    Family and domain databases

    Gene3Di1.10.620.20. 1 hit.
    InterProiIPR009078. Ferritin-like_SF.
    IPR012078. MP_mOase_hydro.
    IPR003430. Phenol_Hydrox.
    IPR012348. RNR-rel.
    [Graphical view]
    PfamiPF02332. Phenol_Hydrox. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000040. MMOH_comp. 1 hit.
    SUPFAMiSSF47240. SSF47240. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P27354-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQPQSSQVT KRGLTDPERA AIIAAAVPDH ALDTQRKYHY FIQPRWKPLS    50
    EYEQLSCYAQ PNPDWIAGGL DWGDWTQKFH GGRPSWGNES TELRTTDWYR 100
    HRDPARRWHH PYVKDKSEEA RYTQRFLAAY SSEGSIRTID PYWRDEILNK 150
    YFGALLYSEY GLFNAHSSVG RDCLSDTIRQ TAVFAALDKV DNAQMIQMER 200
    LFIAKLVPGF DASTDVPKKI WTTDPIYSGA RATVQEIWQG VQDWNEILWA 250
    GHAVMIATFG QFARREFFQR LATVYGDTLT PFFTAQSQTY FQTTRGAIDD 300
    LFVYCLANDS EFGAHNRTFL NAWTEHYLAS SVAALKDFVG LYAKVEKSRA 350
    DRSRRRLRGA AASSAIGRSI TPDKIGFRVD VDQKVDAVLA GYKN 394
    Length:394
    Mass (Da):45,020
    Last modified:January 23, 2007 - v3
    Checksum:iFA6C8F0970F28B90
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55394 Genomic DNA. Translation: CAA39069.1.
    PIRiS15208.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55394 Genomic DNA. Translation: CAA39069.1 .
    PIRi S15208.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MHY X-ray 2.00 B 1-394 [» ]
    1MHZ X-ray 2.70 B 1-394 [» ]
    ProteinModelPortali P27354.
    SMRi P27354. Positions 11-392.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-3868.

    Miscellaneous databases

    EvolutionaryTracei P27354.

    Family and domain databases

    Gene3Di 1.10.620.20. 1 hit.
    InterProi IPR009078. Ferritin-like_SF.
    IPR012078. MP_mOase_hydro.
    IPR003430. Phenol_Hydrox.
    IPR012348. RNR-rel.
    [Graphical view ]
    Pfami PF02332. Phenol_Hydrox. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000040. MMOH_comp. 1 hit.
    SUPFAMi SSF47240. SSF47240. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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 2-16.

    Entry informationi

    Entry nameiMEMB_METTR
    AccessioniPrimary (citable) accession number: P27354
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 77 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3