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Protein

Quinohemoprotein alcohol dehydrogenase

Gene

qheDH

Organism
Comamonas testosteroni (Pseudomonas testosteroni)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the dye-linked oxidation of primary alcohols to the corresponding aldehydes and the (subsequent) oxidation of the aldehydes to carboxylic acids. Methanol is not a substrate.1 Publication1 Publication

Caution

The oxidation form of Trp-543 is subject of controversy and could be the artifactual result of sample handling.1 Publication

Catalytic activityi

A primary alcohol + azurin = an aldehyde + reduced azurin.1 Publication

Cofactori

Protein has several cofactor binding sites:

Kineticsi

  1. KM=5 µM for benzyl alcohol1 Publication
  2. KM=5 µM for butan-1-ol1 Publication
  3. KM=5 µM for pentan-1-ol1 Publication
  4. KM=5 µM for octan-1-ol1 Publication
  5. KM=40 µM for octanal1 Publication
  6. KM=60 µM for propan-1-ol1 Publication
  7. KM=100 µM for butyraldehyde1 Publication
  8. KM=200 µM for 6-aminohexan-1-ol1 Publication
  9. KM=280 µM for butan-1,3-diol1 Publication
  10. KM=900 µM for acetaldehyde1 Publication
  11. KM=3 mM for formaldehyde1 Publication
  12. KM=5 mM for ethanol1 Publication

    pH dependencei

    Optimum pH is 7.7.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei101Pyrroloquinoline quinoneCombined sources1 Publication1
    Binding sitei153Pyrroloquinoline quinoneCombined sources1 Publication1
    Binding sitei198Pyrroloquinoline quinoneCombined sources1 Publication1
    Metal bindingi216CalciumCombined sources1 Publication1
    Binding sitei274Pyrroloquinoline quinoneCombined sources1 Publication1
    Metal bindingi294CalciumCombined sources1 Publication1
    Active sitei339Proton acceptor1 Publication1
    Metal bindingi339CalciumCombined sources1 Publication1
    Binding sitei366Pyrroloquinoline quinoneCombined sources1 Publication1
    Binding sitei575Pyrroloquinoline quinone; via amide nitrogenCombined sources1 Publication1
    Binding sitei635Heme c (covalent)Combined sources1 Publication1
    Binding sitei638Heme c (covalent)Combined sources1 Publication1
    Metal bindingi639Iron (heme axial ligand); via tele nitrogenCombined sources1 Publication1
    Metal bindingi678Iron (heme axial ligand)Combined sources1 Publication1

    GO - Molecular functioni

    Keywordsi

    Molecular functionOxidoreductase
    LigandCalcium, Heme, Iron, Metal-binding, PQQ

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15520
    BRENDAi1.1.9.1 1590

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Quinohemoprotein alcohol dehydrogenase1 Publication (EC:1.1.9.11 Publication)
    Short name:
    QH-ADH1 Publication
    Alternative name(s):
    Alcohol dehydrogenase (azurin)Curated
    PQQ-containing alcohol dehydrogenase1 Publication
    PQQ-dependent ADH1 Publication
    Quinohaemoprotein ethanol dehydrogenase type I1 Publication
    Short name:
    QH-EDHI1 Publication
    Gene namesi
    Name:qheDH1 Publication
    OrganismiComamonas testosteroni (Pseudomonas testosteroni)
    Taxonomic identifieri285 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

    Subcellular locationi

    • Periplasm 1 Publication

    GO - Cellular componenti

    Keywords - Cellular componenti

    Periplasm

    Pathology & Biotechi

    Chemistry databases

    DrugBankiDB03679 2-Hydroxy-Tryptophan
    DB03317 Heme C
    DB03205 Pyrroloquinoline Quinone
    DB03051 Tetrahydrofuran-2-Carboxylic Acid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 312 PublicationsAdd BLAST31
    ChainiPRO_000002556332 – 708Quinohemoprotein alcohol dehydrogenaseAdd BLAST677

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi147 ↔ 148Combined sources1 Publication

    Post-translational modificationi

    In the crystallographic structures Trp-543 is oxidized to 2'-hydroxytryptophan.1 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiQ46444

    Expressioni

    Inductioni

    By ethanol and butanol.1 Publication

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1708
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi33 – 43Combined sources11
    Helixi47 – 52Combined sources6
    Helixi53 – 55Combined sources3
    Turni80 – 82Combined sources3
    Helixi83 – 85Combined sources3
    Beta strandi86 – 93Combined sources8
    Beta strandi105 – 107Combined sources3
    Beta strandi110 – 114Combined sources5
    Helixi116 – 118Combined sources3
    Beta strandi120 – 124Combined sources5
    Turni125 – 127Combined sources3
    Beta strandi130 – 134Combined sources5
    Helixi140 – 145Combined sources6
    Beta strandi146 – 148Combined sources3
    Beta strandi156 – 158Combined sources3
    Beta strandi161 – 165Combined sources5
    Beta strandi169 – 175Combined sources7
    Turni176 – 178Combined sources3
    Beta strandi181 – 186Combined sources6
    Turni187 – 190Combined sources4
    Beta strandi202 – 204Combined sources3
    Beta strandi207 – 210Combined sources4
    Turni215 – 217Combined sources3
    Beta strandi222 – 227Combined sources6
    Turni228 – 230Combined sources3
    Beta strandi233 – 240Combined sources8
    Helixi251 – 257Combined sources7
    Helixi262 – 264Combined sources3
    Turni266 – 269Combined sources4
    Beta strandi279 – 282Combined sources4
    Turni283 – 286Combined sources4
    Beta strandi287 – 291Combined sources5
    Beta strandi295 – 298Combined sources4
    Helixi300 – 303Combined sources4
    Turni311 – 314Combined sources4
    Beta strandi315 – 319Combined sources5
    Turni321 – 323Combined sources3
    Beta strandi326 – 333Combined sources8
    Beta strandi347 – 353Combined sources7
    Beta strandi356 – 363Combined sources8
    Beta strandi368 – 374Combined sources7
    Turni375 – 377Combined sources3
    Beta strandi380 – 387Combined sources8
    Beta strandi390 – 395Combined sources6
    Beta strandi401 – 403Combined sources3
    Helixi405 – 408Combined sources4
    Beta strandi430 – 432Combined sources3
    Turni433 – 436Combined sources4
    Beta strandi437 – 444Combined sources8
    Beta strandi448 – 451Combined sources4
    Helixi467 – 469Combined sources3
    Beta strandi475 – 477Combined sources3
    Beta strandi487 – 494Combined sources8
    Turni495 – 498Combined sources4
    Beta strandi499 – 509Combined sources11
    Beta strandi514 – 517Combined sources4
    Turni518 – 520Combined sources3
    Beta strandi521 – 525Combined sources5
    Beta strandi529 – 535Combined sources7
    Turni536 – 538Combined sources3
    Beta strandi541 – 546Combined sources6
    Beta strandi556 – 560Combined sources5
    Beta strandi563 – 570Combined sources8
    Helixi574 – 579Combined sources6
    Beta strandi590 – 596Combined sources7
    Helixi621 – 623Combined sources3
    Helixi624 – 634Combined sources11
    Helixi636 – 639Combined sources4
    Turni642 – 644Combined sources3
    Beta strandi648 – 650Combined sources3
    Helixi653 – 655Combined sources3
    Helixi658 – 662Combined sources5
    Helixi664 – 668Combined sources5
    Helixi674 – 676Combined sources3
    Turni682 – 684Combined sources3
    Helixi689 – 704Combined sources16

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1KB0X-ray1.44A32-708[»]
    ProteinModelPortaliQ46444
    SMRiQ46444
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ46444

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini619 – 708Cytochrome cPROSITE-ProRule annotationAdd BLAST90

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni214 – 215Pyrroloquinoline quinone bindingCombined sources1 Publication2
    Regioni425 – 426Pyrroloquinoline quinone bindingCombined sources1 Publication2

    Sequence similaritiesi

    Belongs to the bacterial PQQ dehydrogenase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4105DZG Bacteria
    COG4993 LUCA
    KOiK17760

    Family and domain databases

    Gene3Di1.10.760.10, 1 hit
    InterProiView protein in InterPro
    IPR009056 Cyt_c-like_dom
    IPR036909 Cyt_c-like_dom_sf
    IPR018391 PQQ_beta_propeller_repeat
    IPR017512 PQQ_MeOH/EtOH_DH
    IPR002372 PQQ_repeat
    IPR011047 Quinoprotein_ADH-like_supfam
    IPR001479 Quinoprotein_DH_CS
    PfamiView protein in Pfam
    PF13442 Cytochrome_CBB3, 1 hit
    PF13360 PQQ_2, 2 hits
    SMARTiView protein in SMART
    SM00564 PQQ, 5 hits
    SUPFAMiSSF46626 SSF46626, 1 hit
    SSF50998 SSF50998, 1 hit
    TIGRFAMsiTIGR03075 PQQ_enz_alc_DH, 1 hit
    PROSITEiView protein in PROSITE
    PS00364 BACTERIAL_PQQ_2, 1 hit
    PS51007 CYTC, 1 hit

    Sequencei

    Sequence statusi: Complete.

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

    Q46444-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MERLIDNSHG WPGRMVWLLA ACLGSAAAFA QTGPAAQAAA AVQRVDGDFI
    60 70 80 90 100
    RANAARTPDW PTIGVDYAET RYSRLDQINA ANVKDLGLAW SYNLESTRGV
    110 120 130 140 150
    EATPVVVDGI MYVSASWSVV HAIDTRTGNR IWTYDPQIDR STGFKGCCDV
    160 170 180 190 200
    VNRGVALWKG KVYVGAWDGR LIALDAATGK EVWHQNTFEG QKGSLTITGA
    210 220 230 240 250
    PRVFKGKVII GKRGAEYGVR GYITAYDAET GERKWRWFSV PGDPSKPFED
    260 270 280 290 300
    ESMKRAARTW DPSGKWWEAG GGGTMWDSMT FDAELNTMYV GTGNGSPWSH
    310 320 330 340 350
    KVRSPKGGDN LYLASIVALD PDTGKYKWHY QETPGDNWDY TSTQPMILAD
    360 370 380 390 400
    IKIAGKPRKV ILHAPKNGFF FVLDRTNGKF ISAKNFVPVN WASGYDKHGK
    410 420 430 440 450
    PIGIAAARDG SKPQDAVPGP YGAHNWHPMS FNPQTGLVYL PAQNVPVNLM
    460 470 480 490 500
    DDKKWEFNQA GPGKPQSGTG WNTAKFFNAE PPKSKPFGRL LAWDPVAQKA
    510 520 530 540 550
    AWSVEHVSPW NGGTLTTAGN VVFQGTADGR LVAYHAATGE KLWEAPTGTG
    560 570 580 590 600
    VVAAPSTYMV DGRQYVSVAV GWGGVYGLAA RATERQGPGT VYTFVVAGKA
    610 620 630 640 650
    RMPEFVAQRT GQLLQGVKYD PAKVEAGTML YVANCVFCHG VPGVDRGGNI
    660 670 680 690 700
    PNLGYMDASY IENLPNFVFK GPAMVRGMPD FTGKLSGDDV ESLKAFIQGT

    ADAIRPKP
    Length:708
    Mass (Da):76,823
    Last modified:November 1, 1996 - v1
    Checksum:i99AB54BDD6ACCAB3
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X81880 Genomic DNA Translation: CAA57464.1
    PIRiS62366 S52317

    Genome annotation databases

    KEGGiag:CAA57464

    Similar proteinsi

    Entry informationi

    Entry nameiQHED_COMTE
    AccessioniPrimary (citable) accession number: Q46444
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 17, 2003
    Last sequence update: November 1, 1996
    Last modified: May 23, 2018
    This is version 124 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

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