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Protein

Particulate methane monooxygenase alpha subunit

Gene

pmoB1

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

Functioni

Methane monooxygenase is responsible for the initial oxygenation of methane to methanol in methanotrophs. At least in vitro, specific quinols can replace NADH as reductants.3 Publications

Catalytic activityi

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

Cofactori

Cu2+3 PublicationsNote: Binds 3 copper ions per subunit. Two of these (copper ion 1 and 3) form a binuclear cluster.3 Publications

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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi33Copper 11
    Metal bindingi48Copper 21
    Metal bindingi72Copper 21
    Metal bindingi137Copper 31
    Metal bindingi139Copper 11
    Metal bindingi139Copper 31

    GO - Molecular functioni

    Keywordsi

    Molecular functionMonooxygenase, Oxidoreductase
    LigandCopper, Metal-binding, NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-3882.
    BRENDAi1.14.18.3. 10298.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Particulate methane monooxygenase alpha subunit (EC:1.14.18.3)
    Alternative name(s):
    Methane monooxygenase B subunit
    Particulate methane monooxygenase 45 kDa subunit
    Particulate methane monooxygenase 47 kDa subunit
    Particulate methane monooxygenase hydroxylase 45 kDa subunit
    Particulate methane monooxygenase hydroxylase alpha subunit
    Short name:
    pMMO-H alpha subunit
    Gene namesi
    Name:pmoB1
    Synonyms:pmoB
    Ordered Locus Names:MCA1796
    AND
    Name:pmoB2
    Ordered Locus Names:MCA2853
    OrganismiMethylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
    Taxonomic identifieri243233 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaMethylococcalesMethylococcaceaeMethylococcus
    Proteomesi
    • UP000006821 Componenti: Chromosome

    Subcellular locationi

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transmembranei186 – 206HelicalSequence analysisAdd BLAST21
    Transmembranei235 – 255HelicalSequence analysisAdd BLAST21

    GO - Cellular componenti

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi48H → N: Impairs activity of soluble pmoB construct. 1 Publication1
    Mutagenesisi137H → A: Abolishes activity of soluble pmoB construct; when associated with A-139. 1 Publication1
    Mutagenesisi139H → A: Abolishes activity of soluble pmoB construct; when associated with A-137. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 322 PublicationsAdd BLAST32
    ChainiPRO_500014283233 – 414Particulate methane monooxygenase alpha subunitAdd BLAST382

    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.MCA2853.

    Structurei

    Secondary structure

    1414
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi35 – 38Combined sources4
    Helixi40 – 44Combined sources5
    Beta strandi45 – 55Combined sources11
    Beta strandi57 – 60Combined sources4
    Beta strandi64 – 73Combined sources10
    Beta strandi84 – 95Combined sources12
    Beta strandi98 – 105Combined sources8
    Beta strandi121 – 130Combined sources10
    Beta strandi134 – 147Combined sources14
    Beta strandi149 – 161Combined sources13
    Helixi163 – 165Combined sources3
    Beta strandi169 – 171Combined sources3
    Beta strandi177 – 179Combined sources3
    Turni180 – 184Combined sources5
    Helixi185 – 207Combined sources23
    Helixi213 – 220Combined sources8
    Beta strandi225 – 227Combined sources3
    Helixi232 – 254Combined sources23
    Beta strandi281 – 294Combined sources14
    Beta strandi296 – 306Combined sources11
    Beta strandi308 – 310Combined sources3
    Beta strandi312 – 318Combined sources7
    Beta strandi323 – 325Combined sources3
    Turni327 – 329Combined sources3
    Turni338 – 340Combined sources3
    Beta strandi346 – 349Combined sources4
    Beta strandi359 – 367Combined sources9
    Helixi370 – 373Combined sources4
    Helixi376 – 381Combined sources6
    Beta strandi386 – 395Combined sources10
    Beta strandi400 – 408Combined sources9
    Beta strandi410 – 412Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1YEWX-ray2.80A/E/I33-414[»]
    3RGBX-ray2.80A/E/I1-414[»]
    ProteinModelPortaliG1UBD1.
    SMRiG1UBD1.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiG1UBD1.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni33 – 172Cupredoxin domain used to construct soluble pmoB (spmoB)Add BLAST140
    Regioni265 – 414Cupredoxin domain used to construct soluble pmoB (spmoB)Add BLAST150

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiENOG4108P7H. Bacteria.
    ENOG410Y0ZG. LUCA.
    HOGENOMiHOG000029229.
    KOiK10945.
    OMAiLAEDWPR.
    OrthoDBiPOG091H1UXG.

    Family and domain databases

    Gene3Di2.60.120.570. 1 hit.
    InterProiView protein in InterPro
    IPR006833. NH3_CH4_mOase_B.
    IPR023301. NH3_CH4_mOase_suB_N.
    PfamiView protein in Pfam
    PF04744. Monooxygenase_B. 1 hit.
    TIGRFAMsiTIGR03079. CH4_NH3mon_ox_B. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    G1UBD1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKTIKDRIAK WSAIGLLSAV AATAFYAPSA SAHGEKSQAA FMRMRTIHWY
    60 70 80 90 100
    DLSWSKEKVK INETVEIKGK FHVFEGWPET VDEPDVAFLN VGMPGPVFIR
    110 120 130 140 150
    KESYIGGQLV PRSVRLEIGK TYDFRVVLKA RRPGDWHVHT MMNVQGGGPI
    160 170 180 190 200
    IGPGKWITVE GSMSEFRNPV TTLTGQTVDL ENYNEGNTYF WHAFWFAIGV
    210 220 230 240 250
    AWIGYWSRRP IFIPRLLMVD AGRADELVSA TDRKVAMGFL AATILIVVMA
    260 270 280 290 300
    MSSANSKYPI TIPLQAGTMR GMKPLELPAP TVSVKVEDAT YRVPGRAMRM
    310 320 330 340 350
    KLTITNHGNS PIRLGEFYTA SVRFLDSDVY KDTTGYPEDL LAEDGLSVSD
    360 370 380 390 400
    NSPLAPGETR TVDVTASDAA WEVYRLSDII YDPDSRFAGL LFFFDATGNR
    410
    QVVQIDAPLI PSFM
    Length:414
    Mass (Da):46,079
    Last modified:October 19, 2011 - v1
    Checksum:i66AFC0C663F869BA
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L40804 Genomic DNA. Translation: AAB49822.1.
    U94337 Genomic DNA. Translation: AAB51066.1.
    AE017282 Genomic DNA. Translation: AAU91115.1.
    AE017282 Genomic DNA. Translation: AAU92191.1.
    PIRiB57266.
    RefSeqiWP_010961049.1. NC_002977.6.

    Genome annotation databases

    EnsemblBacteriaiAAU91115; AAU91115; MCA2853.
    AAU92191; AAU92191; MCA1796.
    KEGGimca:MCA1796.
    mca:MCA2853.

    Similar proteinsi

    Entry informationi

    Entry nameiPMOB_METCA
    AccessioniPrimary (citable) accession number: G1UBD1
    Secondary accession number(s): O08059, Q49104, Q607G4
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: October 19, 2011
    Last modified: June 7, 2017
    This is version 41 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    A dicopper center located in the alpha/pmoB subunit is proposed as active site, in part based on mutagenesis studies using a soluble pmoB construct in which its two cupredoxin domains have been artificially bridged. However, the construct has only 10% methane oxidation activity compared with the intact membrane-bound pMMO.Curated

    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