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Q53563

- MMOC_METTR

UniProt

Q53563 - MMOC_METTR

Protein

Methane monooxygenase component C

Gene

mmoC

Organism
Methylosinus trichosporium
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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. The component C is the iron-sulfur flavoprotein of sMMO.

    Catalytic activityi

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

    Cofactori

    Binds 1 2Fe-2S cluster.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi37 – 371Iron-sulfur (2Fe-2S)
    Metal bindingi41 – 411Iron-sulfur (2Fe-2S)
    Metal bindingi44 – 441Iron-sulfur (2Fe-2S)
    Metal bindingi76 – 761Iron-sulfur (2Fe-2S)

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi215 – 22915FADBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
    2. electron carrier activity Source: InterPro
    3. metal ion binding Source: UniProtKB-KW
    4. methane monooxygenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. one-carbon metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Electron transport, One-carbon metabolism, Transport

    Keywords - Ligandi

    2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-3870.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methane monooxygenase component C (EC:1.14.13.25)
    Alternative name(s):
    Methane hydroxylase
    Methane monooxygenase reductase
    Short name:
    MMOR
    Gene namesi
    Name:mmoC
    OrganismiMethylosinus trichosporium
    Taxonomic identifieri426 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylocystaceaeMethylosinus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 340340Methane monooxygenase component CPRO_0000189409Add
    BLAST

    Interactioni

    Subunit structurei

    The soluble methane monooxygenase (sMMO) consists of four components A/MMOH (composed of alpha/MmoX, beta/MmoY and gamma/MmoZ), B/MMOB (MmoB), C/MMOR (MmoC) and D/MMOD (MmoD).

    Structurei

    3D structure databases

    ProteinModelPortaliQ53563.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 92922Fe-2S ferredoxin-typeAdd
    BLAST
    Domaini101 – 205105FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di3.10.20.30. 1 hit.
    InterProiIPR001041. 2Fe-2S_ferredoxin-type.
    IPR012675. Beta-grasp_dom.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR008333. OxRdtase_FAD-bd_dom.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR001221. Phe_hydroxylase.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF00970. FAD_binding_6. 1 hit.
    PF00111. Fer2. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view]
    PRINTSiPR00371. FPNCR.
    PR00410. PHEHYDRXLASE.
    SUPFAMiSSF54292. SSF54292. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEiPS51384. FAD_FR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q53563-1 [UniParc]FASTAAdd to Basket

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    MYQIVIETED GETCRRMRPS EDWISRAEAE RNLLASCRAG CATCKADCTD    50
    GDYELIDVKV QAVPPDEEED GKVLLCRTFP RSDLHLLVPY TYDRISFEAI 100
    QTNWLAEILA CDRVSSNVVR LVLQRSRPMA ARISLNFVPG QFVDIEIPGT 150
    HTRRSYSMAS VAEDGQLEFI IRLLPDGAFS KFLQTEAKVG MRVDLRGPAG 200
    SFFLHDHGGR SRVFVAGGTG LSPVLSMIRQ LGKASDPSPA TLLFGVTNRE 250
    ELFYVDELKT LAQSMPTLGV RIAVVNDDGG NGVDKGTVID LLRAELEIDL 300
    LLGHARRRRR RETARSCRED HRDRCPAWRS DFLEKFLASG 340
    Length:340
    Mass (Da):37,991
    Last modified:November 1, 1996 - v1
    Checksum:i79AE21DA8079E6D8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S81887 Genomic DNA. Translation: AAB21393.1.
    PIRiC48360.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S81887 Genomic DNA. Translation: AAB21393.1 .
    PIRi C48360.

    3D structure databases

    ProteinModelPortali Q53563.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-3870.

    Family and domain databases

    Gene3Di 3.10.20.30. 1 hit.
    InterProi IPR001041. 2Fe-2S_ferredoxin-type.
    IPR012675. Beta-grasp_dom.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR008333. OxRdtase_FAD-bd_dom.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR001221. Phe_hydroxylase.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view ]
    Pfami PF00970. FAD_binding_6. 1 hit.
    PF00111. Fer2. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00371. FPNCR.
    PR00410. PHEHYDRXLASE.
    SUPFAMi SSF54292. SSF54292. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEi PS51384. FAD_FR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The methane monooxygenase gene cluster of Methylosinus trichosporium: cloning and sequencing of the mmoC gene."
      Cardy D.L.N., Laidler V., Salmond G.P.C., Murrell J.C.
      Arch. Microbiol. 156:477-483(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 1-13, CHARACTERIZATION, COMPLEX FORMATION.
      Strain: OB3b.

    Entry informationi

    Entry nameiMMOC_METTR
    AccessioniPrimary (citable) accession number: Q53563
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 6, 2002
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3