Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P11987

- MEMG_METCA

UniProt

P11987 - MEMG_METCA

Protein

Methane monooxygenase component A gamma chain

Gene

mmoZ

Organism
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. methane 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-3863.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methane monooxygenase component A gamma chain (EC:1.14.13.25)
    Alternative name(s):
    Methane hydroxylase
    Gene namesi
    Name:mmoZ
    Ordered Locus Names:MCA1198
    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 – 170169Methane monooxygenase component A gamma chainPRO_0000096409Add
    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-59863N.
    STRINGi243233.MCA1198.

    Structurei

    Secondary structure

    1
    170
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 83
    Helixi10 – 2011
    Helixi25 – 3915
    Turni48 – 525
    Helixi53 – 7119
    Helixi74 – 796
    Helixi87 – 10014
    Helixi104 – 11815
    Turni119 – 1224
    Helixi125 – 14319
    Turni144 – 1485
    Helixi152 – 1598
    Beta strandi162 – 1676

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FYZX-ray2.15E/F1-170[»]
    1FZ0X-ray2.07E/F1-170[»]
    1FZ1X-ray1.96E/F1-170[»]
    1FZ2X-ray2.15E/F1-170[»]
    1FZ3X-ray2.03E/F1-170[»]
    1FZ4X-ray2.38E/F1-170[»]
    1FZ5X-ray2.40E/F1-170[»]
    1FZ6X-ray2.05E/F1-170[»]
    1FZ7X-ray1.96E/F1-170[»]
    1FZ8X-ray2.10E/F1-170[»]
    1FZ9X-ray2.30E/F1-170[»]
    1FZHX-ray2.60E/F1-170[»]
    1FZIX-ray3.30E/F1-170[»]
    1MMOX-ray2.20G/H4-165[»]
    1MTYX-ray1.70G/H4-165[»]
    1XMFX-ray2.32E/F2-170[»]
    1XMGX-ray2.10E/F2-170[»]
    1XMHX-ray2.32E/F2-170[»]
    1XU3X-ray2.30E/F1-170[»]
    1XU5X-ray1.96E/F1-170[»]
    1XVBX-ray1.80E/F1-170[»]
    1XVCX-ray2.00E/F1-170[»]
    1XVDX-ray2.30E/F1-170[»]
    1XVEX-ray2.40E/F1-170[»]
    1XVFX-ray2.00E/F1-170[»]
    1XVGX-ray1.96E/F1-170[»]
    4GAMX-ray2.90C/H/M/R1-170[»]
    ProteinModelPortaliP11987.
    SMRiP11987. Positions 3-170.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11987.

    Family & Domainsi

    Phylogenomic databases

    eggNOGiNOG257614.
    HOGENOMiHOG000086317.
    KOiK16159.
    OMAiQHEETER.
    OrthoDBiEOG6SV5J6.

    Family and domain databases

    Gene3Di1.20.1280.10. 1 hit.
    1.20.1280.30. 1 hit.
    InterProiIPR004222. Me_mOase_g.
    IPR015952. Me_mOase_g_dom1.
    IPR015953. Me_mOase_g_dom2.
    [Graphical view]
    PfamiPF02964. MeMO_Hyd_G. 1 hit.
    [Graphical view]
    PIRSFiPIRSF018503. Me_mOase_g. 1 hit.
    ProDomiPD022203. Me_mOase_g. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF47152. SSF47152. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P11987-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKLGIHSND TRDAWVNKIA QLNTLEKAAE MLKQFRMDHT TPFRNSYELD    50
    NDYLWIEAKL EEKVAVLKAR AFNEVDFRHK TAFGEDAKSV LDGTVAKMNA 100
    AKDKWEAEKI HIGFRQAYKP PIMPVNYFLD GERQLGTRLM ELRNLNYYDT 150
    PLEELRKQRG VRVVHLQSPH 170
    Length:170
    Mass (Da):19,847
    Last modified:January 23, 2007 - v4
    Checksum:i6030AF38130BA497
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211Q → E AA sequence 1 PublicationCurated
    Sequence conflicti26 – 261E → Q AA sequence 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M90050 Genomic DNA. Translation: AAF04157.2.
    AE017282 Genomic DNA. Translation: AAU92724.1.
    PIRiJL0102.
    RefSeqiWP_010960485.1. NC_002977.6.
    YP_113663.1. NC_002977.6.

    Genome annotation databases

    EnsemblBacteriaiAAU92724; AAU92724; MCA1198.
    GeneIDi3102570.
    KEGGimca:MCA1198.
    PATRICi22606228. VBIMetCap22254_1230.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M90050 Genomic DNA. Translation: AAF04157.2 .
    AE017282 Genomic DNA. Translation: AAU92724.1 .
    PIRi JL0102.
    RefSeqi WP_010960485.1. NC_002977.6.
    YP_113663.1. 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 E/F 1-170 [» ]
    1FZ0 X-ray 2.07 E/F 1-170 [» ]
    1FZ1 X-ray 1.96 E/F 1-170 [» ]
    1FZ2 X-ray 2.15 E/F 1-170 [» ]
    1FZ3 X-ray 2.03 E/F 1-170 [» ]
    1FZ4 X-ray 2.38 E/F 1-170 [» ]
    1FZ5 X-ray 2.40 E/F 1-170 [» ]
    1FZ6 X-ray 2.05 E/F 1-170 [» ]
    1FZ7 X-ray 1.96 E/F 1-170 [» ]
    1FZ8 X-ray 2.10 E/F 1-170 [» ]
    1FZ9 X-ray 2.30 E/F 1-170 [» ]
    1FZH X-ray 2.60 E/F 1-170 [» ]
    1FZI X-ray 3.30 E/F 1-170 [» ]
    1MMO X-ray 2.20 G/H 4-165 [» ]
    1MTY X-ray 1.70 G/H 4-165 [» ]
    1XMF X-ray 2.32 E/F 2-170 [» ]
    1XMG X-ray 2.10 E/F 2-170 [» ]
    1XMH X-ray 2.32 E/F 2-170 [» ]
    1XU3 X-ray 2.30 E/F 1-170 [» ]
    1XU5 X-ray 1.96 E/F 1-170 [» ]
    1XVB X-ray 1.80 E/F 1-170 [» ]
    1XVC X-ray 2.00 E/F 1-170 [» ]
    1XVD X-ray 2.30 E/F 1-170 [» ]
    1XVE X-ray 2.40 E/F 1-170 [» ]
    1XVF X-ray 2.00 E/F 1-170 [» ]
    1XVG X-ray 1.96 E/F 1-170 [» ]
    4GAM X-ray 2.90 C/H/M/R 1-170 [» ]
    ProteinModelPortali P11987.
    SMRi P11987. Positions 3-170.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59863N.
    STRINGi 243233.MCA1198.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAU92724 ; AAU92724 ; MCA1198 .
    GeneIDi 3102570.
    KEGGi mca:MCA1198.
    PATRICi 22606228. VBIMetCap22254_1230.

    Phylogenomic databases

    eggNOGi NOG257614.
    HOGENOMi HOG000086317.
    KOi K16159.
    OMAi QHEETER.
    OrthoDBi EOG6SV5J6.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-3863.

    Miscellaneous databases

    EvolutionaryTracei P11987.

    Family and domain databases

    Gene3Di 1.20.1280.10. 1 hit.
    1.20.1280.30. 1 hit.
    InterProi IPR004222. Me_mOase_g.
    IPR015952. Me_mOase_g_dom1.
    IPR015953. Me_mOase_g_dom2.
    [Graphical view ]
    Pfami PF02964. MeMO_Hyd_G. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF018503. Me_mOase_g. 1 hit.
    ProDomi PD022203. Me_mOase_g. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF47152. SSF47152. 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].
      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 21-22.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 33009 / NCIMB 11132 / Bath.
    4. "Cloning of the gamma-subunit methane monooxygenase from Methylococcus capsulatus."
      Mullens I.A., Dalton H.
      Biotechnology (N.Y.) 5:490-493(1987)
      Cited for: PROTEIN SEQUENCE OF 2-40.
    5. "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] OF 166-170.
      Strain: ATCC 33009 / NCIMB 11132 / Bath.
    6. "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 nameiMEMG_METCA
    AccessioniPrimary (citable) accession number: P11987
    Secondary accession number(s): Q609N4, Q9RLQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 105 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