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P27353

- MEMA_METTR

UniProt

P27353 - MEMA_METTR

Protein

Methane monooxygenase component A alpha chain

Gene

mmoX

Organism
Methylosinus trichosporium
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 4 (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.

    Cofactori

    Binds 2 iron ions.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi114 – 1141Iron 1By similarity
    Metal bindingi144 – 1441Iron 1By similarity
    Metal bindingi147 – 1471Iron 1By similarity
    Active sitei151 – 1511Sequence Analysis
    Metal bindingi209 – 2091Iron 2By similarity
    Metal bindingi243 – 2431Iron 2By similarity
    Metal bindingi246 – 2461Iron 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. 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

    Iron, Metal-binding, NADP

    Names & Taxonomyi

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 526525Methane monooxygenase component A alpha chainPRO_0000096406Add
    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
    526
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi25 – 295
    Helixi30 – 356
    Helixi64 – 8320
    Helixi85 – 884
    Helixi91 – 933
    Helixi97 – 12731
    Helixi131 – 16131
    Turni166 – 1705
    Helixi171 – 1744
    Helixi175 – 1773
    Helixi179 – 18810
    Helixi190 – 1934
    Helixi197 – 2048
    Turni205 – 2073
    Helixi208 – 2114
    Helixi213 – 22614
    Helixi231 – 25727
    Helixi261 – 29232
    Helixi301 – 3088
    Helixi309 – 3157
    Helixi316 – 3205
    Helixi321 – 3244
    Helixi332 – 3387
    Turni339 – 3413
    Helixi342 – 35211
    Helixi354 – 3563
    Beta strandi357 – 3604
    Helixi366 – 37510
    Turni377 – 3826
    Helixi383 – 39311
    Turni394 – 3963
    Helixi398 – 4003
    Helixi404 – 4107
    Turni419 – 4213
    Turni427 – 4293
    Beta strandi437 – 4415
    Beta strandi444 – 4485
    Helixi451 – 4599
    Helixi461 – 4633
    Helixi469 – 4735
    Helixi478 – 4847
    Beta strandi492 – 4965
    Beta strandi498 – 5003
    Beta strandi502 – 5043
    Helixi509 – 5146
    Helixi522 – 5254

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MHYX-ray2.00D1-525[»]
    1MHZX-ray2.70D1-525[»]
    ProteinModelPortaliP27353.
    SMRiP27353. Positions 17-526.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27353.

    Family & Domainsi

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

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

    P27353-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAISLATKAA TDALKVNRAP VGVEPQEVHK WLQSFNWDFK ENRTKYPTKY    50
    HMANETKEQF KVIAKEYARM EAAKDERQFG TLLDGLTRLG AGNKVHPRWG 100
    ETMKVISNFL EVGEYNAIAA SAMLWDSATA AEQKNGYLAQ VLDEIRHTHQ 150
    CAFINHYYSK HYHDPAGHND ARRTRAIGPL WKGMKRVFAD GFISGDAVEC 200
    SVNLQLVGEA CFTNPLIVAV TEWASANGDE ITPTVFLSVE TDELRHMANG 250
    YQTVVSIAND PASAKFLNTD LNNAFWTQQK YFTPVLGYLF EYGSKFKVEP 300
    WVKTWNRWVY EDWGGIWIGR LGKYGVESPA SLRDAKRDAY WAHHDLALAA 350
    YAMWPLGFAR LALPDEEDQA WFEANYPGWA DHYGKIFNEW KKLGYEDPKS 400
    GFIPYQWLLA NGHDVYIDRV SQVPFIPSLA KGTGSLRVHE FNGKKHSLTD 450
    DWGERQWLIE PERYECHNVF EQYEGRELSE VIAEGHGVRS DGKTLIAQPH 500
    TRGDNLWTLE DIKRAGCVFP DPLAKF 526
    Length:526
    Mass (Da):59,954
    Last modified:January 23, 2007 - v4
    Checksum:iA56F4AAD0A55726B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55394 Genomic DNA. Translation: CAA39068.2.
    PIRiS15207.

    Genome annotation databases

    PATRICi38005870. VBIMetTri17036_0736.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55394 Genomic DNA. Translation: CAA39068.2 .
    PIRi S15207.

    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 D 1-525 [» ]
    1MHZ X-ray 2.70 D 1-525 [» ]
    ProteinModelPortali P27353.
    SMRi P27353. Positions 17-526.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    PATRICi 38005870. VBIMetTri17036_0736.

    Miscellaneous databases

    EvolutionaryTracei P27353.

    Family and domain databases

    Gene3Di 1.10.620.20. 1 hit.
    InterProi IPR009078. Ferritin-like_SF.
    IPR003430. Phenol_Hydrox.
    IPR012348. RNR-rel.
    [Graphical view ]
    Pfami PF02332. Phenol_Hydrox. 1 hit.
    [Graphical view ]
    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. McDonald I.
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "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 nameiMEMA_METTR
    AccessioniPrimary (citable) accession number: P27353
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 83 of the entry and version 4 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