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P38539

- DHM1_METME

UniProt

P38539 - DHM1_METME

Protein

Methanol dehydrogenase [cytochrome c] subunit 1

Gene
N/A
Organism
Methylophilus methylotrophus (Bacterium W3A1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (08 Nov 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidation of primary alcohols including methanol.

    Catalytic activityi

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

    Cofactori

    Binds 1 calcium ion per subunit.
    Binds 1 PQQ per subunit. PQQ is inserted between disulfide Cys-105-Cys-106 and the indole ring of Trp-239.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi173 – 1731Calcium
    Metal bindingi257 – 2571Calcium
    Active sitei299 – 2991Proton acceptor

    GO - Molecular functioni

    1. 2-chloroethanol cytochrome-c oxidoreductase activity Source: UniProtKB-EC
    2. calcium ion binding 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 metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Methanol utilization

    Keywords - Ligandi

    Calcium, Metal-binding, PQQ

    Enzyme and pathway databases

    SABIO-RKP38539.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methanol dehydrogenase [cytochrome c] subunit 1 (EC:1.1.2.7)
    Alternative name(s):
    MDH large subunit alpha
    MEDH
    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. outer membrane-bounded periplasmic space Source: InterPro
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 573573Methanol dehydrogenase [cytochrome c] subunit 1PRO_0000205342Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi105 ↔ 106
    Disulfide bondi146 ↔ 169
    Disulfide bondi381 ↔ 410

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Heterotetramer of 2 alpha and 2 beta subunits.

    Structurei

    Secondary structure

    1
    573
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 107
    Turni36 – 383
    Helixi39 – 413
    Beta strandi43 – 497
    Beta strandi61 – 633
    Beta strandi66 – 705
    Turni73 – 753
    Beta strandi77 – 815
    Beta strandi87 – 926
    Helixi98 – 1036
    Beta strandi114 – 1163
    Beta strandi119 – 1235
    Beta strandi127 – 1337
    Turni134 – 1363
    Beta strandi139 – 1446
    Helixi148 – 1503
    Beta strandi159 – 1613
    Beta strandi164 – 1685
    Helixi172 – 1743
    Beta strandi179 – 1846
    Turni185 – 1873
    Beta strandi190 – 1989
    Helixi200 – 2034
    Turni207 – 2126
    Helixi214 – 2163
    Helixi221 – 2244
    Helixi230 – 2334
    Beta strandi243 – 2453
    Turni246 – 2494
    Beta strandi250 – 2545
    Beta strandi259 – 2613
    Helixi263 – 2653
    Turni271 – 2744
    Beta strandi275 – 2806
    Turni281 – 2833
    Beta strandi286 – 2938
    Beta strandi307 – 3137
    Beta strandi316 – 3249
    Beta strandi328 – 3347
    Turni335 – 3373
    Beta strandi340 – 3478
    Beta strandi352 – 3565
    Turni358 – 3603
    Beta strandi362 – 3654
    Helixi367 – 3693
    Beta strandi377 – 3826
    Beta strandi394 – 3963
    Turni397 – 4004
    Beta strandi401 – 4077
    Beta strandi409 – 4157
    Beta strandi429 – 4357
    Beta strandi446 – 4516
    Turni453 – 4553
    Beta strandi458 – 4669
    Beta strandi473 – 4753
    Turni476 – 4783
    Beta strandi479 – 4835
    Beta strandi487 – 4937
    Turni494 – 4963
    Beta strandi499 – 5046
    Beta strandi514 – 5185
    Beta strandi521 – 5288
    Turni532 – 5354
    Helixi536 – 5394
    Helixi547 – 5504
    Helixi551 – 5544
    Turni555 – 5573
    Helixi558 – 5603
    Beta strandi567 – 5726

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G72X-ray1.90A/C1-573[»]
    2AD6X-ray1.50A/C3-573[»]
    2AD7X-ray1.50A/C3-573[»]
    2AD8X-ray1.60A/C3-573[»]
    4AAHX-ray2.40A/C3-573[»]
    ProteinModelPortaliP38539.
    SMRiP38539. Positions 3-573.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38539.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the bacterial PQQ dehydrogenase family.Curated

    Family and domain databases

    Gene3Di2.140.10.10. 1 hit.
    InterProiIPR018391. PQQ_beta_propeller_repeat.
    IPR017512. PQQ_MeOH/EtOH_DH.
    IPR002372. PQQ_repeat.
    IPR027295. Quinonprotein_ADH-like_fam.
    IPR011047. Quinonprotein_ADH-like_supfam.
    IPR001479. Quinoprotein_DH_CS.
    [Graphical view]
    PfamiPF01011. PQQ. 5 hits.
    [Graphical view]
    SMARTiSM00564. PQQ. 4 hits.
    [Graphical view]
    SUPFAMiSSF50998. SSF50998. 1 hit.
    TIGRFAMsiTIGR03075. PQQ_enz_alc_DH. 1 hit.
    PROSITEiPS00364. BACTERIAL_PQQ_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38539-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADADLDKQV NTAGAWPIAT GGYYSQHNSP LAQINKSNVK NVKAAWSFST    50
    GVLNGHEGAP LVIGDMMYVH SAFPNNTYAL NLNDPGKIVW QHKPKQDAST 100
    KAVMCCDVVD RGLAYGAGQI VKKQANGHLL ALDAKTGKIN WEVEVCDPKV 150
    GSTLTQAPFV AKDTVLMGCS GAELGVRGAV NAFDLKTGEL KWRAFATGSD 200
    DSVRLAKDFN SANPHYGQFG LGTKTWEGDA WKIGGGTNWG WYAYDPKLNL 250
    FYYGSGNPAP WNETMRPGDN KWTMTIWGRD LDTGMAKWGY QKTPHDEWDF 300
    AGVNQMVLTD QPVNGKMTPL LSHIDRNGIL YTLNRENGNL IVAEKVDPAV 350
    NVFKKVDLKT GTPVRDPEFA TRMDHKGTNI CPSAMGFHNQ GVDSYDPESR 400
    TLYAGLNHIC MDWEPFMLPY RAGQFFVGAT LAMYPGPNGP TKKEMGQIRA 450
    FDLTTGKAKW TKWEKFAAWG GTLYTKGGLV WYATLDGYLK ALDNKDGKEL 500
    WNFKMPSGGI GSPMTYSFKG KQYIGSMYGV GGWPGVGLVF DLTDPSAGLG 550
    AVGAFRELQN HTQMGGGLMV FSL 573
    Length:573
    Mass (Da):62,635
    Last modified:November 8, 2002 - v2
    Checksum:iA06C9B3091BB8F0C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U41040 Genomic DNA. Translation: AAA83765.1.
    PIRiS68591.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U41040 Genomic DNA. Translation: AAA83765.1 .
    PIRi S68591.

    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 A/C 1-573 [» ]
    2AD6 X-ray 1.50 A/C 3-573 [» ]
    2AD7 X-ray 1.50 A/C 3-573 [» ]
    2AD8 X-ray 1.60 A/C 3-573 [» ]
    4AAH X-ray 2.40 A/C 3-573 [» ]
    ProteinModelPortali P38539.
    SMRi P38539. Positions 3-573.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P38539.

    Miscellaneous databases

    EvolutionaryTracei P38539.

    Family and domain databases

    Gene3Di 2.140.10.10. 1 hit.
    InterProi IPR018391. PQQ_beta_propeller_repeat.
    IPR017512. PQQ_MeOH/EtOH_DH.
    IPR002372. PQQ_repeat.
    IPR027295. Quinonprotein_ADH-like_fam.
    IPR011047. Quinonprotein_ADH-like_supfam.
    IPR001479. Quinoprotein_DH_CS.
    [Graphical view ]
    Pfami PF01011. PQQ. 5 hits.
    [Graphical view ]
    SMARTi SM00564. PQQ. 4 hits.
    [Graphical view ]
    SUPFAMi SSF50998. SSF50998. 1 hit.
    TIGRFAMsi TIGR03075. PQQ_enz_alc_DH. 1 hit.
    PROSITEi PS00364. BACTERIAL_PQQ_2. 1 hit.
    [Graphical view ]
    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. "Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes."
      Anthony C.
      Antioxid. Redox Signal. 3:757-774(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    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 nameiDHM1_METME
    AccessioniPrimary (citable) accession number: P38539
    Secondary accession number(s): Q59540
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: November 8, 2002
    Last modified: October 1, 2014
    This is version 102 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

    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