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P38540

- DHM2_METME

UniProt

P38540 - DHM2_METME

Protein

Methanol dehydrogenase [cytochrome c] subunit 2

Gene

moxI

Organism
Methylophilus methylotrophus (Bacterium W3A1)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Catalyzes the oxidation of primary alcohols including methanol.By similarity

    Catalytic activityi

    A primary alcohol + 2 cytochrome c(L) = an aldehyde + 2 reduced cytochrome c(L) + 2 H+.

    GO - Molecular functioni

    1. 2-chloroethanol cytochrome-c oxidoreductase activity Source: UniProtKB-EC
    2. alcohol dehydrogenase (NAD) activity Source: InterPro
    3. ethanol cytochrome-c oxidoreductase activity Source: UniProtKB-EC
    4. methanol ferricytochrome-c oxidoreductase activity Source: UniProtKB-EC

    GO - Biological processi

    1. methanol oxidation Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Methanol utilization

    Enzyme and pathway databases

    SABIO-RKP38540.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methanol dehydrogenase [cytochrome c] subunit 2 (EC:1.1.2.7)
    Alternative name(s):
    MDH small subunit beta
    MDH-associated peptide
    MEDH
    Gene namesi
    Name:moxI
    OrganismiMethylophilus methylotrophus (Bacterium W3A1)
    Taxonomic identifieri17 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaMethylophilalesMethylophilaceaeMethylophilus

    Subcellular locationi

    Cell inner membrane; Peripheral membrane protein; Periplasmic side
    Note: Periplasmic, but associated with inner membrane.

    GO - Cellular componenti

    1. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 9169Methanol dehydrogenase [cytochrome c] subunit 2PRO_0000025570Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 34

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Heterotetramer composed of 2 alpha and 2 beta subunits.

    Structurei

    Secondary structure

    1
    91
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi56 – 594
    Helixi61 – 8323

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G72X-ray1.90B/D23-91[»]
    2AD6X-ray1.50B/D23-91[»]
    2AD7X-ray1.50B/D23-91[»]
    2AD8X-ray1.60B/D23-91[»]
    4AAHX-ray2.40B/D23-91[»]
    ProteinModelPortaliP38540.
    SMRiP38540. Positions 23-91.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38540.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di4.10.160.10. 1 hit.
    InterProiIPR003420. Meth_DH_bsu.
    [Graphical view]
    PfamiPF02315. MDH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF029163. Meth_DH_beta. 1 hit.
    SUPFAMiSSF48666. SSF48666. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P38540-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKHVLTLLAL ASVFAVSNQA LAYDGQNCKE PGNCWENKPG YPEKIAGSKY   50
    DPKHDPVELN KQEESIKAMD ARNAKRIANA KSSGNFVFDV K 91
    Length:91
    Mass (Da):10,037
    Last modified:November 8, 2002 - v2
    Checksum:i0123300087E6716A
    GO

    Sequence cautioni

    The sequence AAA83766.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 271N → T AA sequence (PubMed:1311606)Curated
    Sequence conflicti31 – 311P → A AA sequence (PubMed:1311606)Curated
    Sequence conflicti37 – 371N → A AA sequence (PubMed:1311606)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U41041 Genomic DNA. Translation: AAA83766.1. Different initiation.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U41041 Genomic DNA. Translation: AAA83766.1 . Different initiation.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G72 X-ray 1.90 B/D 23-91 [» ]
    2AD6 X-ray 1.50 B/D 23-91 [» ]
    2AD7 X-ray 1.50 B/D 23-91 [» ]
    2AD8 X-ray 1.60 B/D 23-91 [» ]
    4AAH X-ray 2.40 B/D 23-91 [» ]
    ProteinModelPortali P38540.
    SMRi P38540. Positions 23-91.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P38540.

    Miscellaneous databases

    EvolutionaryTracei P38540.

    Family and domain databases

    Gene3Di 4.10.160.10. 1 hit.
    InterProi IPR003420. Meth_DH_bsu.
    [Graphical view ]
    Pfami PF02315. MDH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF029163. Meth_DH_beta. 1 hit.
    SUPFAMi SSF48666. SSF48666. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Determination of the gene sequence and the three-dimensional structure at 2.4 angstroms resolution of methanol dehydrogenase from Methylophilus W3A1."
      Xia Z.-X., Dai W.-W., Zhang Y.-F., White S.A., Boyd G.D., Mathews F.S.
      J. Mol. Biol. 259:480-501(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    2. "The interaction of methanol dehydrogenase and its electron acceptor, cytochrome cL in methylotrophic bacteria."
      Cox J.M., Day D.J., Anthony C.
      Biochim. Biophys. Acta 1119:97-106(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-53.
      Strain: ATCC 53528 / AS1 / DSM 46235 / LMG 6787 / NCIMB 10515.
    3. "The active site structure of the calcium-containing quinoprotein methanol dehydrogenase."
      White S.A., Boyd G.D., Mathews F.S., Xia Z.-X., Dai W.-W., Zhang Y.-F., Davidson V.L.
      Biochemistry 32:12955-12958(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    4. "The three-dimensional structures of methanol dehydrogenase from two methylotrophic bacteria at 2.6-A resolution."
      Xia Z.-X., Dai W.-W., Xiong J.-P., Hao Z.-P., Davidson V.L., White S.A., Mathews F.S.
      J. Biol. Chem. 267:22289-22297(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

    Entry informationi

    Entry nameiDHM2_METME
    AccessioniPrimary (citable) accession number: P38540
    Secondary accession number(s): Q59541
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: November 8, 2002
    Last modified: October 1, 2014
    This is version 88 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, Direct protein sequencing

    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