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Protein

Particulate methane monooxygenase beta subunit

Gene

pmoA1

more
Organism
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Non-catalytic subunit of the methane monooxygenase that is responsible for the initial oxygenation of methane to methanol in methanotrophs. At least in vitro, specific quinols can replace NADH as reductants.2 Publications

Catalytic activityi

Methane + quinol + O2 = methanol + quinone + H2O.1 Publication

Kineticsi

Kinetic parameters have been established with the pMMO heteromeric complex.

    1. Vmax=24.2 nmol/min/mg enzyme (with NADH as reductant)1 Publication
    2. Vmax=4.4 nmol/min/mg enzyme (with decyl-plastoquinol as reductant)1 Publication
    3. Vmax=2.9 nmol/min/mg enzyme (with duroquinol as reductant)1 Publication

    GO - Molecular functioni

    • methane monooxygenase activity Source: JCVI

    GO - Biological processi

    • methane metabolic process Source: JCVI
    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-3881.
    BRENDAi1.14.18.3. 3305.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Particulate methane monooxygenase beta subunit (EC:1.14.18.3)
    Alternative name(s):
    Methane monooxygenase A subunit
    Particulate methane monooxygenase 27 kDa subunit
    Particulate methane monooxygenase hydroxylase 26 kDa subunit
    Particulate methane monooxygenase hydroxylase beta subunit
    Short name:
    pMMO-H beta subunit
    Gene namesi
    Name:pmoA1
    Synonyms:pmoA
    Ordered Locus Names:MCA1797
    AND
    Name:pmoA2
    Ordered Locus Names:MCA2854
    OrganismiMethylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
    Taxonomic identifieri243233 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaMethylococcalesMethylococcaceaeMethylococcus
    Proteomesi
    • UP000006821 Componenti: Chromosome

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei23 – 4321HelicalSequence analysisAdd
    BLAST
    Transmembranei59 – 7921HelicalSequence analysisAdd
    BLAST
    Transmembranei86 – 10621HelicalSequence analysisAdd
    BLAST
    Transmembranei111 – 13121HelicalSequence analysisAdd
    BLAST
    Transmembranei145 – 16521HelicalSequence analysisAdd
    BLAST
    Transmembranei215 – 23521HelicalSequence analysisAdd
    BLAST

    GO - Cellular componenti

    • integral component of membrane Source: UniProtKB-KW
    • methane monooxygenase complex Source: JCVI
    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 247247Particulate methane monooxygenase beta subunitPRO_0000419131Add
    BLAST

    Interactioni

    Subunit structurei

    M.capsulatus has two forms of methane monooxygenase, a soluble (sMMO) and a membrane-bound (particulate) type (pMMO). The particulate type is a nonamer composed of three alpha:beta:gamma heterotrimeric protomers assembled into a cylindrical structure; the beta and gamma subunits comprise the bulk of the membrane-spanning regions and the soluble regions are derived primarily from alpha subunits which form two antiparallel beta-barrel-like structures each. This assembly, also called pMMO hydroxylase (pMMO-H), is proposed to associate with methanol dehydrogenase (MDH), also designated as pMMO-R, to form the pMMO-C complex which seems to have greater methane monooxygenase activity.6 Publications

    Protein-protein interaction databases

    STRINGi243233.MCA2854.

    Structurei

    Secondary structure

    1
    247
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 4331Combined sources
    Beta strandi48 – 503Combined sources
    Helixi52 – 543Combined sources
    Helixi59 – 6810Combined sources
    Helixi70 – 8314Combined sources
    Helixi88 – 10619Combined sources
    Helixi107 – 1115Combined sources
    Helixi116 – 1194Combined sources
    Helixi125 – 13612Combined sources
    Helixi141 – 16424Combined sources
    Helixi165 – 1684Combined sources
    Beta strandi170 – 1734Combined sources
    Beta strandi176 – 1794Combined sources
    Helixi180 – 1878Combined sources
    Turni200 – 2056Combined sources
    Turni208 – 2103Combined sources
    Helixi215 – 23824Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YEWX-ray2.80B/F/J1-247[»]
    3RGBX-ray2.80B/F/J1-247[»]
    ProteinModelPortaliQ607G3.
    SMRiQ607G3. Positions 7-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ607G3.

    Family & Domainsi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiENOG4105E7Z. Bacteria.
    ENOG4110CTU. LUCA.
    HOGENOMiHOG000029228.
    KOiK10944.
    OMAiDWKDRQW.
    OrthoDBiEOG6Z6FQJ.

    Family and domain databases

    Gene3Di1.20.1450.10. 1 hit.
    InterProiIPR003393. NH3_CH4_mOase_A.
    [Graphical view]
    PfamiPF02461. AMO. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR03080. CH4_NH3mon_ox_A. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q607G3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSAAQSAVRS HAEAVQVSRT IDWMALFVVF FVIVGSYHIH AMLTMGDWDF
    60 70 80 90 100
    WSDWKDRRLW VTVTPIVLVT FPAAVQSYLW ERYRLPWGAT VCVLGLLLGE
    110 120 130 140 150
    WINRYFNFWG WTYFPINFVF PASLVPGAII LDTVLMLSGS YLFTAIVGAM
    160 170 180 190 200
    GWGLIFYPGN WPIIAPLHVP VEYNGMLMSI ADIQGYNYVR TGTPEYIRMV
    210 220 230 240
    EKGTLRTFGK DVAPVSAFFS AFMSILIYFM WHFIGRWFSN ERFLQST
    Length:247
    Mass (Da):28,425
    Last modified:November 23, 2004 - v1
    Checksum:i3341AA1A46A53F8F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 171Missing AA sequence (PubMed:9525893).Curated
    Sequence conflicti173 – 1731Y → N (PubMed:7768803).Curated
    Sequence conflicti173 – 1731Y → N in AAB49821 (PubMed:10376840).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L40804 Genomic DNA. Translation: AAB49821.1.
    U94337 Genomic DNA. Translation: AAB51065.1.
    AE017282 Genomic DNA. Translation: AAU91114.1.
    AE017282 Genomic DNA. Translation: AAU92182.1.
    RefSeqiWP_010961050.1. NC_002977.6.

    Genome annotation databases

    EnsemblBacteriaiAAU91114; AAU91114; MCA2854.
    AAU92182; AAU92182; MCA1797.
    KEGGimca:MCA1797.
    mca:MCA2854.
    PATRICi22607436. VBIMetCap22254_1826.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L40804 Genomic DNA. Translation: AAB49821.1.
    U94337 Genomic DNA. Translation: AAB51065.1.
    AE017282 Genomic DNA. Translation: AAU91114.1.
    AE017282 Genomic DNA. Translation: AAU92182.1.
    RefSeqiWP_010961050.1. NC_002977.6.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YEWX-ray2.80B/F/J1-247[»]
    3RGBX-ray2.80B/F/J1-247[»]
    ProteinModelPortaliQ607G3.
    SMRiQ607G3. Positions 7-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi243233.MCA2854.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAU91114; AAU91114; MCA2854.
    AAU92182; AAU92182; MCA1797.
    KEGGimca:MCA1797.
    mca:MCA2854.
    PATRICi22607436. VBIMetCap22254_1826.

    Phylogenomic databases

    eggNOGiENOG4105E7Z. Bacteria.
    ENOG4110CTU. LUCA.
    HOGENOMiHOG000029228.
    KOiK10944.
    OMAiDWKDRQW.
    OrthoDBiEOG6Z6FQJ.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-3881.
    BRENDAi1.14.18.3. 3305.

    Miscellaneous databases

    EvolutionaryTraceiQ607G3.

    Family and domain databases

    Gene3Di1.20.1450.10. 1 hit.
    InterProiIPR003393. NH3_CH4_mOase_A.
    [Graphical view]
    PfamiPF02461. AMO. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR03080. CH4_NH3mon_ox_A. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Particulate methane monooxygenase genes in methanotrophs."
      Semrau J.D., Chistoserdov A., Lebron J., Costello A., Davagnino J., Kenna E., Holmes A.J., Finch R., Murrell J.C., Lidstrom M.E.
      J. Bacteriol. 177:3071-3079(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 33009 / NCIMB 11132 / Bath.
    2. "Role of multiple gene copies in particulate methane monooxygenase activity in the methane-oxidizing bacterium Methylococcus capsulatus Bath."
      Stolyar S., Costello A.M., Peeples T.L., Lidstrom M.E.
      Microbiology 145:1235-1244(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: ATCC 33009 / NCIMB 11132 / Bath.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 33009 / NCIMB 11132 / Bath.
    4. "The particulate methane monooxygenase from methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme. Isolation and characterization."
      Nguyen H.H., Elliott S.J., Yip J.H., Chan S.I.
      J. Biol. Chem. 273:7957-7966(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 6-33, SUBUNIT.
    5. "Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors."
      Shiemke A.K., Cook S.A., Miley T., Singleton P.
      Arch. Biochem. Biophys. 321:421-428(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    6. "The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein."
      Basu P., Katterle B., Andersson K.K., Dalton H.
      Biochem. J. 369:417-427(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUBUNIT.
    7. "Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath)."
      Kitmitto A., Myronova N., Basu P., Dalton H.
      Biochemistry 44:10954-10965(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ELECTRON MICROSCOPY, SUBUNIT.
    8. "Three-dimensional structure determination of a protein supercomplex that oxidizes methane to formaldehyde in Methylococcus capsulatus (Bath)."
      Myronova N., Kitmitto A., Collins R.F., Miyaji A., Dalton H.
      Biochemistry 45:11905-11914(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CRYOELECTRON MICROSCOPY, SUBUNIT.
    9. "Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane."
      Lieberman R.L., Rosenzweig A.C.
      Nature 434:177-182(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), SUBUNIT, SUBCELLULAR LOCATION.
    10. "Crystal structure and characterization of particulate methane monooxygenase from Methylocystis species strain M."
      Smith S.M., Rawat S., Telser J., Hoffman B.M., Stemmler T.L., Rosenzweig A.C.
      Biochemistry 50:10231-10240(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), SUBUNIT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiPMOA_METCA
    AccessioniPrimary (citable) accession number: Q607G3
    Secondary accession number(s): G1U9W5, O05112, Q49103
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: November 23, 2004
    Last modified: December 9, 2015
    This is version 81 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Products of both gene copies, pmoA1 and pmoA2, are required for full cellular activity.

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.