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Protein

Quinoprotein alcohol dehydrogenase (cytochrome c)

Gene

exaA

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of primary alcohols to the corresponding aldehydes, except for methanol, which is a very poor substrate. ExaA is also able to use secondary alcohols as well as amino alcohols like ethanolamine and l-amino-2-propanol, and aldehydes as substrates.1 Publication

Catalytic activityi

A primary alcohol + 2 cytochrome c = an aldehyde + 2 reduced cytochrome c + 2 H+.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • pyrroloquinoline quinone2 PublicationsNote: Binds 1 PQQ group per subunit (PubMed:3144289, PubMed:10736230). PQQ is inserted between disulfide Cys-139-Cys-140 and the plane of Trp-282.2 Publications
  • Ca2+1 Publication1 PublicationNote: Binds 2 calcium ions per subunit.1 Publication

Enzyme regulationi

Inhibited by cyclopropanone ethylhemiketal. Activated by ammonia (500mM), methylamine (5mM), ethylamine (5mM), octylamine (5mM), ethanolamine (5mM) and 1-amino-2-propanol (5mM).1 Publication

Kineticsi

  1. KM=14 µM for ethanol1 Publication
  2. KM=21 µM for 1-propanol1 Publication
  3. KM=680 µM for 2-propanol1 Publication
  4. KM=980 µM for S+-2-butanol1 Publication
  5. KM=4.5 mM for ethanal1 Publication
  6. KM=94 mM for methanol1 Publication

    pH dependencei

    Optimum pH is 9.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi45Calcium 1Combined sources1 Publication1
    Metal bindingi48Calcium 1Combined sources1 Publication1
    Metal bindingi51Calcium 1Combined sources1 Publication1
    Binding sitei95Pyrroloquinoline quinoneCombined sources1 Publication1
    Binding sitei145Pyrroloquinoline quinoneCombined sources1 Publication1
    Binding sitei189Pyrroloquinoline quinoneCombined sources1 Publication1
    Metal bindingi213Calcium 2Combined sources1 Publication1
    Metal bindingi300Calcium 2Combined sources1 Publication1
    Active sitei350Proton acceptor1 Publication1
    Metal bindingi350Calcium 2Combined sources1 Publication1
    Binding sitei378Pyrroloquinoline quinoneCombined sources1 Publication1
    Binding sitei523Pyrroloquinoline quinoneCombined sources1 Publication1
    Binding sitei587Pyrroloquinoline quinone; via amide nitrogenCombined sources1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    • ethanol oxidation Source: PseudoCAP

    Keywordsi

    Molecular functionOxidoreductase
    LigandCalcium, Metal-binding, PQQ

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15517.
    PAER208964:G1FZ6-2020-MONOMER.
    BRENDAi1.1.2.8. 5087.
    1.1.2.B3. 5087.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Quinoprotein alcohol dehydrogenase (cytochrome c)Curated (EC:1.1.2.81 Publication)
    Alternative name(s):
    Quinoprotein alcohol dehydrogenase (cytochrome c550)Curated
    Quinoprotein ethanol dehydrogenase1 Publication
    Short name:
    QEDH1 Publication
    Gene namesi
    Name:exaA1 Publication
    Ordered Locus Names:PA1982
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    Proteomesi
    • UP000002438 Componenti: Chromosome

    Organism-specific databases

    PseudoCAPiPA1982.

    Subcellular locationi

    • Periplasm 1 Publication

    GO - Cellular componenti

    Keywords - Cellular componenti

    Periplasm

    Pathology & Biotechi

    Chemistry databases

    DrugBankiDB03205. Pyrroloquinoline Quinone.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 341 Publication1 PublicationAdd BLAST34
    ChainiPRO_000002556535 – 623Quinoprotein alcohol dehydrogenase (cytochrome c)Add BLAST589

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi139 ↔ 140Combined sources1 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiQ9Z4J7.
    PRIDEiQ9Z4J7.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Protein-protein interaction databases

    STRINGi208964.PA1982.

    Structurei

    Secondary structure

    1623
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi39 – 43Combined sources5
    Helixi45 – 47Combined sources3
    Turni72 – 74Combined sources3
    Helixi75 – 77Combined sources3
    Beta strandi79 – 85Combined sources7
    Beta strandi99 – 101Combined sources3
    Beta strandi104 – 109Combined sources6
    Turni110 – 112Combined sources3
    Beta strandi113 – 121Combined sources9
    Beta strandi124 – 129Combined sources6
    Beta strandi148 – 150Combined sources3
    Beta strandi153 – 158Combined sources6
    Turni159 – 161Combined sources3
    Beta strandi162 – 170Combined sources9
    Beta strandi173 – 178Combined sources6
    Helixi182 – 184Combined sources3
    Beta strandi193 – 196Combined sources4
    Turni198 – 200Combined sources3
    Beta strandi203 – 207Combined sources5
    Helixi212 – 214Combined sources3
    Beta strandi219 – 223Combined sources5
    Turni225 – 227Combined sources3
    Beta strandi230 – 237Combined sources8
    Beta strandi241 – 244Combined sources4
    Beta strandi247 – 253Combined sources7
    Helixi272 – 276Combined sources5
    Beta strandi286 – 288Combined sources3
    Turni289 – 292Combined sources4
    Beta strandi293 – 298Combined sources6
    Beta strandi301 – 304Combined sources4
    Helixi306 – 309Combined sources4
    Beta strandi325 – 330Combined sources6
    Turni332 – 334Combined sources3
    Beta strandi337 – 344Combined sources8
    Beta strandi358 – 363Combined sources6
    Beta strandi365 – 367Combined sources3
    Beta strandi369 – 376Combined sources8
    Beta strandi380 – 386Combined sources7
    Turni387 – 389Combined sources3
    Beta strandi392 – 400Combined sources9
    Beta strandi404 – 408Combined sources5
    Turni410 – 412Combined sources3
    Beta strandi415 – 417Combined sources3
    Beta strandi436 – 440Combined sources5
    Turni455 – 457Combined sources3
    Beta strandi460 – 465Combined sources6
    Beta strandi467 – 473Combined sources7
    Beta strandi487 – 494Combined sources8
    Beta strandi499 – 505Combined sources7
    Turni507 – 509Combined sources3
    Beta strandi512 – 520Combined sources9
    Beta strandi527 – 529Combined sources3
    Turni530 – 532Combined sources3
    Beta strandi533 – 537Combined sources5
    Beta strandi541 – 547Combined sources7
    Turni548 – 550Combined sources3
    Beta strandi553 – 558Combined sources6
    Beta strandi568 – 572Combined sources5
    Beta strandi575 – 582Combined sources8
    Helixi587 – 591Combined sources5
    Helixi594 – 599Combined sources6
    Beta strandi607 – 612Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1FLGX-ray2.60A/B35-616[»]
    ProteinModelPortaliQ9Z4J7.
    SMRiQ9Z4J7.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Z4J7.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni207 – 209Pyrroloquinoline quinone bindingCombined sources1 Publication3

    Sequence similaritiesi

    Belongs to the bacterial PQQ dehydrogenase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4105DZG. Bacteria.
    COG4993. LUCA.
    HOGENOMiHOG000217981.
    InParanoidiQ9Z4J7.
    KOiK00114.
    OMAiWNTWART.
    PhylomeDBiQ9Z4J7.

    Family and domain databases

    CDDicd10277. PQQ_ADH_I. 1 hit.
    InterProiView protein in InterPro
    IPR034119. ADHI.
    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
    PF01011. PQQ. 1 hit.
    PF13360. PQQ_2. 1 hit.
    SMARTiView protein in SMART
    SM00564. PQQ. 6 hits.
    SUPFAMiSSF50998. SSF50998. 1 hit.
    TIGRFAMsiTIGR03075. PQQ_enz_alc_DH. 1 hit.
    PROSITEiView protein in PROSITE
    PS00363. BACTERIAL_PQQ_1. 1 hit.
    PS00364. BACTERIAL_PQQ_2. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9Z4J7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTTRTSPAPA GLLRPSLHCL AFAVALGSAG AALAKDVTWE DIANDDKTTG
    60 70 80 90 100
    DVLQYGMGTH AQRWSPLKQV NADNVFKLTP AWSYSFGDEK QRGQESQAIV
    110 120 130 140 150
    SDGVIYVTAS YSRLFALDAK TGKRLWTYNH RLPDDIRPCC DVVNRGAAIY
    160 170 180 190 200
    GDKVFFGTLD ASVVALNKNT GKVVWKKKFA DHGAGYTMTG APTIVKDGKT
    210 220 230 240 250
    GKVLLIHGSS GDEFGVVGRL FARDPDTGEE IWMRPFVEGH MGRLNGKDST
    260 270 280 290 300
    VTGDVKAPSW PDDRNSPTGK VESWSHGGGA PWQSASFDAE TNTIIVGAGN
    310 320 330 340 350
    PGPWNTWART AKGGNPHDYD SLYTSGQVGV DPSSGEVKWF YQHTPNDAWD
    360 370 380 390 400
    FSGNNELVLF DYKAKDGKIV KATAHADRNG FFYVVDRSNG KLQNAFPFVD
    410 420 430 440 450
    NITWASHIDL KTGRPVEREG QRPPLPEPGQ KHGKAVEVSP PFLGGKNWNP
    460 470 480 490 500
    MAYSQDTGLF YVPANHWKED YWTEEVSYTK GSAYLGMGFR IKRMYDDHVG
    510 520 530 540 550
    SLRAMDPVSG KVVWEHKEHL PLWAGVLATA GNLVFTGTGD GYFKAFDAKS
    560 570 580 590 600
    GKELWKFQTG SGIVSPPITW EQDGEQYLGV TVGYGGAVPL WGGDMADLTR
    610 620
    PVAQGGSFWV FKLPSWDNRT ASR
    Length:623
    Mass (Da):68,123
    Last modified:May 1, 1999 - v1
    Checksum:i32DDE5DF20B291D6
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ009858 Genomic DNA. Translation: CAA08896.1.
    AE004091 Genomic DNA. Translation: AAG05370.1.
    AF068264 Genomic DNA. Translation: AAC79657.1.
    PIRiB83399.
    RefSeqiNP_250672.1. NC_002516.2.
    WP_003088524.1. NC_002516.2.

    Genome annotation databases

    EnsemblBacteriaiAAG05370; AAG05370; PA1982.
    GeneIDi880475.
    KEGGipae:PA1982.
    PATRICifig|208964.12.peg.2066.

    Similar proteinsi

    Entry informationi

    Entry nameiEXAA_PSEAE
    AccessioniPrimary (citable) accession number: Q9Z4J7
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1999
    Last modified: February 28, 2018
    This is version 132 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, Complete proteome, Direct protein sequencing, Reference proteome