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P18798

- MEMB_METCA

UniProt

P18798 - MEMB_METCA

Protein

Methane monooxygenase component A beta chain

Gene

mmoY

Organism
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (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.

    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-3862.

    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
    Ordered Locus Names:MCA1195
    OrganismiMethylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
    Taxonomic identifieri243233 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaMethylococcalesMethylococcaceaeMethylococcus
    ProteomesiUP000006821: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 389388Methane monooxygenase component A beta chainPRO_0000096407Add
    BLAST

    Interactioni

    Subunit structurei

    M.capsulatus 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.

    Protein-protein interaction databases

    DIPiDIP-59862N.
    STRINGi243233.MCA1195.

    Structurei

    Secondary structure

    1
    389
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni10 – 123
    Helixi14 – 2310
    Turni35 – 384
    Beta strandi42 – 454
    Helixi48 – 536
    Helixi85 – 873
    Helixi95 – 973
    Helixi106 – 12924
    Helixi132 – 1354
    Helixi138 – 1425
    Helixi143 – 1475
    Helixi148 – 16114
    Helixi164 – 1696
    Helixi173 – 20331
    Helixi212 – 2209
    Beta strandi222 – 2243
    Helixi225 – 23612
    Helixi241 – 25010
    Helixi252 – 26211
    Helixi265 – 2684
    Helixi269 – 2724
    Helixi276 – 29924
    Helixi300 – 3045
    Turni307 – 3093
    Helixi310 – 33526
    Helixi336 – 3416
    Helixi349 – 36214
    Helixi368 – 3714
    Helixi377 – 3859
    Turni386 – 3883

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FYZX-ray2.15C/D1-389[»]
    1FZ0X-ray2.07C/D1-389[»]
    1FZ1X-ray1.96C/D1-389[»]
    1FZ2X-ray2.15C/D1-389[»]
    1FZ3X-ray2.03C/D1-389[»]
    1FZ4X-ray2.38C/D1-389[»]
    1FZ5X-ray2.40C/D1-389[»]
    1FZ6X-ray2.05C/D1-389[»]
    1FZ7X-ray1.96C/D1-389[»]
    1FZ8X-ray2.10C/D1-389[»]
    1FZ9X-ray2.30C/D1-389[»]
    1FZHX-ray2.60C/D1-389[»]
    1FZIX-ray3.30C/D1-389[»]
    1MMOX-ray2.20B/C6-389[»]
    1MTYX-ray1.70B/C6-362[»]
    1XMFX-ray2.32C/D2-389[»]
    1XMGX-ray2.10C/D2-389[»]
    1XMHX-ray2.32C/D2-389[»]
    1XU3X-ray2.30C/D1-389[»]
    1XU5X-ray1.96C/D1-389[»]
    1XVBX-ray1.80C/D1-389[»]
    1XVCX-ray2.00C/D1-389[»]
    1XVDX-ray2.30C/D1-389[»]
    1XVEX-ray2.40C/D1-389[»]
    1XVFX-ray2.00C/D1-389[»]
    1XVGX-ray1.96C/D1-389[»]
    4GAMX-ray2.90B/G/L/Q1-389[»]
    ProteinModelPortaliP18798.
    SMRiP18798. Positions 2-389.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP18798.

    Family & Domainsi

    Phylogenomic databases

    eggNOGiNOG268646.
    HOGENOMiHOG000086315.
    KOiK16158.
    OMAiKAEEWRY.
    OrthoDBiEOG679T94.

    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.

    P18798-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSMLGERRRG LTDPEMAAVI LKALPEAPLD GNNKMGYFVT PRWKRLTEYE    50
    ALTVYAQPNA DWIAGGLDWG DWTQKFHGGR PSWGNETTEL RTVDWFKHRD 100
    PLRRWHAPYV KDKAEEWRYT DRFLQGYSAD GQIRAMNPTW RDEFINRYWG 150
    AFLFNEYGLF NAHSQGAREA LSDVTRVSLA FWGFDKIDIA QMIQLERGFL 200
    AKIVPGFDES TAVPKAEWTN GEVYKSARLA VEGLWQEVFD WNESAFSVHA 250
    VYDALFGQFV RREFFQRLAP RFGDNLTPFF INQAQTYFQI AKQGVQDLYY 300
    NCLGDDPEFS DYNRTVMRNW TGKWLEPTIA ALRDFMGLFA KLPAGTTDKE 350
    EITASLYRVV DDWIEDYASR IDFKADRDQI VKAVLAGLK 389
    Length:389
    Mass (Da):45,133
    Last modified:January 23, 2007 - v4
    Checksum:i1737FEA30EEA9875
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti370 – 3701R → A in AAB62393. (PubMed:2505721)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M90050 Genomic DNA. Translation: AAB62393.2.
    AE017282 Genomic DNA. Translation: AAU92727.1.
    PIRiA61412.
    JL0101.
    RefSeqiWP_010960483.1. NC_002977.6.
    YP_113660.1. NC_002977.6.

    Genome annotation databases

    EnsemblBacteriaiAAU92727; AAU92727; MCA1195.
    GeneIDi3103426.
    KEGGimca:MCA1195.
    PATRICi22606222. VBIMetCap22254_1227.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M90050 Genomic DNA. Translation: AAB62393.2 .
    AE017282 Genomic DNA. Translation: AAU92727.1 .
    PIRi A61412.
    JL0101.
    RefSeqi WP_010960483.1. NC_002977.6.
    YP_113660.1. NC_002977.6.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FYZ X-ray 2.15 C/D 1-389 [» ]
    1FZ0 X-ray 2.07 C/D 1-389 [» ]
    1FZ1 X-ray 1.96 C/D 1-389 [» ]
    1FZ2 X-ray 2.15 C/D 1-389 [» ]
    1FZ3 X-ray 2.03 C/D 1-389 [» ]
    1FZ4 X-ray 2.38 C/D 1-389 [» ]
    1FZ5 X-ray 2.40 C/D 1-389 [» ]
    1FZ6 X-ray 2.05 C/D 1-389 [» ]
    1FZ7 X-ray 1.96 C/D 1-389 [» ]
    1FZ8 X-ray 2.10 C/D 1-389 [» ]
    1FZ9 X-ray 2.30 C/D 1-389 [» ]
    1FZH X-ray 2.60 C/D 1-389 [» ]
    1FZI X-ray 3.30 C/D 1-389 [» ]
    1MMO X-ray 2.20 B/C 6-389 [» ]
    1MTY X-ray 1.70 B/C 6-362 [» ]
    1XMF X-ray 2.32 C/D 2-389 [» ]
    1XMG X-ray 2.10 C/D 2-389 [» ]
    1XMH X-ray 2.32 C/D 2-389 [» ]
    1XU3 X-ray 2.30 C/D 1-389 [» ]
    1XU5 X-ray 1.96 C/D 1-389 [» ]
    1XVB X-ray 1.80 C/D 1-389 [» ]
    1XVC X-ray 2.00 C/D 1-389 [» ]
    1XVD X-ray 2.30 C/D 1-389 [» ]
    1XVE X-ray 2.40 C/D 1-389 [» ]
    1XVF X-ray 2.00 C/D 1-389 [» ]
    1XVG X-ray 1.96 C/D 1-389 [» ]
    4GAM X-ray 2.90 B/G/L/Q 1-389 [» ]
    ProteinModelPortali P18798.
    SMRi P18798. Positions 2-389.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59862N.
    STRINGi 243233.MCA1195.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAU92727 ; AAU92727 ; MCA1195 .
    GeneIDi 3103426.
    KEGGi mca:MCA1195.
    PATRICi 22606222. VBIMetCap22254_1227.

    Phylogenomic databases

    eggNOGi NOG268646.
    HOGENOMi HOG000086315.
    KOi K16158.
    OMAi KAEEWRY.
    OrthoDBi EOG679T94.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-3862.

    Miscellaneous databases

    EvolutionaryTracei P18798.

    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 methane monooxygenase from Methylococcus capsulatus (Bath)."
      Stainthorpe A.C., Murrell J.C., Salmond G.P.C., Dalton H., Lees V.
      Arch. Microbiol. 152:154-159(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-41.
      Strain: ATCC 33009 / NCIMB 11132 / Bath.
    2. McDonald I., Murrell J.C.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 142-145 AND C-TERMINUS.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 33009 / NCIMB 11132 / Bath.
    4. "Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane."
      Rosenzweig A.C., Frederick C.A., Lippard S.J., Nordlund P.
      Nature 366:537-543(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

    Entry informationi

    Entry nameiMEMB_METCA
    AccessioniPrimary (citable) accession number: P18798
    Secondary accession number(s): Q609N7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 110 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, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3