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P22868

- MMOC_METCA

UniProt

P22868 - MMOC_METCA

Protein

Methane monooxygenase component C

Gene

mmoC

Organism
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (26 Sep 2001)
      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 bindingi42 – 421Iron-sulfur (2Fe-2S)
    Metal bindingi47 – 471Iron-sulfur (2Fe-2S)
    Metal bindingi50 – 501Iron-sulfur (2Fe-2S)
    Metal bindingi82 – 821Iron-sulfur (2Fe-2S)

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi221 – 23515FADBy 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-3864.

    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
    Ordered Locus Names:MCA1200
    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
    Chaini1 – 348348Methane monooxygenase component CPRO_0000189408Add
    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).

    Protein-protein interaction databases

    STRINGi243233.MCA1200.

    Structurei

    Secondary structure

    1
    348
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 118
    Turni12 – 143
    Beta strandi15 – 239
    Helixi27 – 348
    Beta strandi54 – 563
    Turni66 – 683
    Helixi71 – 777
    Turni81 – 833
    Beta strandi90 – 934
    Beta strandi106 – 1138
    Beta strandi117 – 1204
    Beta strandi123 – 1286
    Beta strandi134 – 1385
    Beta strandi147 – 1504
    Beta strandi156 – 1616
    Beta strandi167 – 1704
    Beta strandi173 – 1775
    Beta strandi183 – 1853
    Helixi186 – 1927
    Beta strandi193 – 20513
    Beta strandi214 – 2163
    Beta strandi218 – 2258
    Helixi228 – 24013
    Beta strandi246 – 2516
    Beta strandi253 – 2553
    Helixi261 – 27010
    Beta strandi271 – 2733
    Beta strandi275 – 2784
    Beta strandi288 – 2958
    Helixi296 – 3049
    Beta strandi305 – 31612
    Helixi317 – 33014
    Beta strandi335 – 3395
    Beta strandi343 – 3453

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JQ4NMR-A1-98[»]
    1TVCNMR-A99-348[»]
    DisProtiDP00379.
    ProteinModelPortaliP22868.
    SMRiP22868. Positions 1-348.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22868.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 98942Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini106 – 211106FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
    Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0543.
    HOGENOMiHOG000263663.
    KOiK16161.
    OMAiILMCRTT.
    OrthoDBiEOG6RNQ9P.

    Family and domain databases

    Gene3Di3.10.20.30. 1 hit.
    InterProiIPR001041. 2Fe-2S_ferredoxin-type.
    IPR006058. 2Fe2S_fd_BS.
    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.
    PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
    PS51085. 2FE2S_FER_2. 1 hit.
    PS51384. FAD_FR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P22868-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQRVHTITAV TEDGESLRFE CRSDEDVITA ALRQNIFLMS SCREGGCATC    50
    KALCSEGDYD LKGCSVQALP PEEEEEGLVL LCRTYPKTDL EIELPYTHCR 100
    ISFGEVGSFE AEVVGLNWVS SNTVQFLLQK RPDECGNRGV KFEPGQFMDL 150
    TIPGTDVSRS YSPANLPNPE GRLEFLIRVL PEGRFSDYLR NDARVGQVLS 200
    VKGPLGVFGL KERGMAPRYF VAGGTGLAPV VSMVRQMQEW TAPNETRIYF 250
    GVNTEPELFY IDELKSLERS MRNLTVKACV WHPSGDWEGE QGSPIDALRE 300
    DLESSDANPD IYLCGPPGMI DAACELVRSR GIPGEQVFFE KFLPSGAA 348
    Length:348
    Mass (Da):38,542
    Last modified:September 26, 2001 - v2
    Checksum:i7577BEB408CA1C1F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M90050 Genomic DNA. Translation: AAB62391.2.
    AE017282 Genomic DNA. Translation: AAU92722.1.
    PIRiJQ0701.
    RefSeqiWP_010960487.1. NC_002977.6.
    YP_113665.1. NC_002977.6.

    Genome annotation databases

    EnsemblBacteriaiAAU92722; AAU92722; MCA1200.
    GeneIDi3103263.
    KEGGimca:MCA1200.
    PATRICi22606232. VBIMetCap22254_1232.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M90050 Genomic DNA. Translation: AAB62391.2 .
    AE017282 Genomic DNA. Translation: AAU92722.1 .
    PIRi JQ0701.
    RefSeqi WP_010960487.1. NC_002977.6.
    YP_113665.1. NC_002977.6.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JQ4 NMR - A 1-98 [» ]
    1TVC NMR - A 99-348 [» ]
    DisProti DP00379.
    ProteinModelPortali P22868.
    SMRi P22868. Positions 1-348.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243233.MCA1200.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAU92722 ; AAU92722 ; MCA1200 .
    GeneIDi 3103263.
    KEGGi mca:MCA1200.
    PATRICi 22606232. VBIMetCap22254_1232.

    Phylogenomic databases

    eggNOGi COG0543.
    HOGENOMi HOG000263663.
    KOi K16161.
    OMAi ILMCRTT.
    OrthoDBi EOG6RNQ9P.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-3864.

    Miscellaneous databases

    EvolutionaryTracei P22868.

    Family and domain databases

    Gene3Di 3.10.20.30. 1 hit.
    InterProi IPR001041. 2Fe-2S_ferredoxin-type.
    IPR006058. 2Fe2S_fd_BS.
    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 PS00197. 2FE2S_FER_1. 1 hit.
    PS51085. 2FE2S_FER_2. 1 hit.
    PS51384. FAD_FR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath)."
      Stainthorpe A.C., Lees V., Salmond G.P.C., Dalton H., Murrell J.C.
      Gene 91:27-34(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-16.
      Strain: ATCC 33009 / NCIMB 11132 / Bath.
    2. McDonald I., Murrell J.C.
      Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 254.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 33009 / NCIMB 11132 / Bath.
    4. "NMR structure of the [2Fe-2S] ferredoxin domain from soluble methane monooxygenase reductase and interaction with its hydroxylase."
      Mueller J., Lugovskoy A.A., Wagner G., Lippard S.J.
      Biochemistry 41:42-51(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
      Strain: ATCC 33009 / NCIMB 11132 / Bath.

    Entry informationi

    Entry nameiMMOC_METCA
    AccessioniPrimary (citable) accession number: P22868
    Secondary accession number(s): Q609N2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: September 26, 2001
    Last modified: October 1, 2014
    This is version 121 of the entry and version 2 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
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3