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Protein

Quinohemoprotein ethanol dehydrogenase type-1

Gene

qheDH

Organism
Comamonas testosteroni (Pseudomonas testosteroni)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi216 – 2161Calcium
Metal bindingi294 – 2941Calcium
Binding sitei635 – 6351Heme (covalent)
Binding sitei638 – 6381Heme (covalent)
Metal bindingi639 – 6391Iron (heme axial ligand)

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding, PQQ

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15520.
BRENDAi1.1.9.1. 1590.

Names & Taxonomyi

Protein namesi
Recommended name:
Quinohemoprotein ethanol dehydrogenase type-1 (EC:1.1.9.1)
Alternative name(s):
Alcohol dehydrogenase (azurin)
QH-EDH1
Quinohemoprotein ethanol dehydrogenase type I
Gene namesi
Name:qheDH
OrganismiComamonas testosteroni (Pseudomonas testosteroni)
Taxonomic identifieri285 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 31311 PublicationAdd
BLAST
Chaini32 – 708677Quinohemoprotein ethanol dehydrogenase type-1PRO_0000025563Add
BLAST

Post-translational modificationi

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

Expressioni

Inductioni

By ethanol and butanol.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi399795.CtesDRAFT_PD4908.

Structurei

Secondary structure

1
708
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 4311Combined sources
Helixi47 – 526Combined sources
Helixi53 – 553Combined sources
Turni80 – 823Combined sources
Helixi83 – 853Combined sources
Beta strandi86 – 938Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi110 – 1145Combined sources
Helixi116 – 1183Combined sources
Beta strandi120 – 1245Combined sources
Turni125 – 1273Combined sources
Beta strandi130 – 1345Combined sources
Helixi140 – 1456Combined sources
Beta strandi146 – 1483Combined sources
Beta strandi156 – 1583Combined sources
Beta strandi161 – 1655Combined sources
Beta strandi169 – 1757Combined sources
Turni176 – 1783Combined sources
Beta strandi181 – 1866Combined sources
Turni187 – 1904Combined sources
Beta strandi202 – 2043Combined sources
Beta strandi207 – 2104Combined sources
Turni215 – 2173Combined sources
Beta strandi222 – 2276Combined sources
Turni228 – 2303Combined sources
Beta strandi233 – 2408Combined sources
Helixi251 – 2577Combined sources
Helixi262 – 2643Combined sources
Turni266 – 2694Combined sources
Beta strandi279 – 2824Combined sources
Turni283 – 2864Combined sources
Beta strandi287 – 2915Combined sources
Beta strandi295 – 2984Combined sources
Helixi300 – 3034Combined sources
Turni311 – 3144Combined sources
Beta strandi315 – 3195Combined sources
Turni321 – 3233Combined sources
Beta strandi326 – 3338Combined sources
Beta strandi347 – 3537Combined sources
Beta strandi356 – 3638Combined sources
Beta strandi368 – 3747Combined sources
Turni375 – 3773Combined sources
Beta strandi380 – 3878Combined sources
Beta strandi390 – 3956Combined sources
Beta strandi401 – 4033Combined sources
Helixi405 – 4084Combined sources
Beta strandi430 – 4323Combined sources
Turni433 – 4364Combined sources
Beta strandi437 – 4448Combined sources
Beta strandi448 – 4514Combined sources
Helixi467 – 4693Combined sources
Beta strandi475 – 4773Combined sources
Beta strandi487 – 4948Combined sources
Turni495 – 4984Combined sources
Beta strandi499 – 50911Combined sources
Beta strandi514 – 5174Combined sources
Turni518 – 5203Combined sources
Beta strandi521 – 5255Combined sources
Beta strandi529 – 5357Combined sources
Turni536 – 5383Combined sources
Beta strandi541 – 5466Combined sources
Beta strandi556 – 5605Combined sources
Beta strandi563 – 5708Combined sources
Helixi574 – 5796Combined sources
Beta strandi590 – 5967Combined sources
Helixi621 – 6233Combined sources
Helixi624 – 63411Combined sources
Helixi636 – 6394Combined sources
Turni642 – 6443Combined sources
Beta strandi648 – 6503Combined sources
Helixi653 – 6553Combined sources
Helixi658 – 6625Combined sources
Helixi664 – 6685Combined sources
Helixi674 – 6763Combined sources
Turni682 – 6843Combined sources
Helixi689 – 70416Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KB0X-ray1.44A32-708[»]
ProteinModelPortaliQ46444.
SMRiQ46444. Positions 32-706.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ46444.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini619 – 70890Cytochrome cPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the bacterial PQQ dehydrogenase family.Curated
Contains 1 cytochrome c domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105DZG. Bacteria.
COG4993. LUCA.
KOiK17760.

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
2.140.10.10. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR018391. PQQ_beta_propeller_repeat.
IPR017512. PQQ_MeOH/EtOH_DH.
IPR002372. PQQ_repeat.
IPR027295. Quinoprotein_ADH-like_fam.
IPR011047. Quinoprotein_ADH-like_supfam.
IPR001479. Quinoprotein_DH_CS.
[Graphical view]
PfamiPF13442. Cytochrome_CBB3. 1 hit.
PF13360. PQQ_2. 2 hits.
[Graphical view]
SMARTiSM00564. PQQ. 5 hits.
[Graphical view]
SUPFAMiSSF46626. SSF46626. 1 hit.
SSF50998. SSF50998. 1 hit.
TIGRFAMsiTIGR03075. PQQ_enz_alc_DH. 1 hit.
PROSITEiPS00364. BACTERIAL_PQQ_2. 1 hit.
PS51007. CYTC. 1 hit.
[Graphical view]

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.

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KB0X-ray1.44A32-708[»]
ProteinModelPortaliQ46444.
SMRiQ46444. Positions 32-706.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi399795.CtesDRAFT_PD4908.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA57464.

Phylogenomic databases

eggNOGiENOG4105DZG. Bacteria.
COG4993. LUCA.
KOiK17760.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15520.
BRENDAi1.1.9.1. 1590.

Miscellaneous databases

EvolutionaryTraceiQ46444.

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
2.140.10.10. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR018391. PQQ_beta_propeller_repeat.
IPR017512. PQQ_MeOH/EtOH_DH.
IPR002372. PQQ_repeat.
IPR027295. Quinoprotein_ADH-like_fam.
IPR011047. Quinoprotein_ADH-like_supfam.
IPR001479. Quinoprotein_DH_CS.
[Graphical view]
PfamiPF13442. Cytochrome_CBB3. 1 hit.
PF13360. PQQ_2. 2 hits.
[Graphical view]
SMARTiSM00564. PQQ. 5 hits.
[Graphical view]
SUPFAMiSSF46626. SSF46626. 1 hit.
SSF50998. SSF50998. 1 hit.
TIGRFAMsiTIGR03075. PQQ_enz_alc_DH. 1 hit.
PROSITEiPS00364. BACTERIAL_PQQ_2. 1 hit.
PS51007. CYTC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of the gene encoding quinohaemoprotein ethanol dehydrogenase of Comamonas testosteroni."
    Stoorvogel J., Kraayveld D.E., van Sluis C.A., Jongejan J.A., De Vries S., Duine J.A.
    Eur. J. Biochem. 235:690-698(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 15667 / JCM 13048 / LMG 7106 / NCIB 9682.
  2. "Quinohaemoprotein ethanol dehydrogenase from Comamonas testosteroni. Purification, characterization, and reconstitution of the apoenzyme with pyrroloquinoline quinone analogues."
    de Jong G.A.H., Geerlof A., Stoorvogel J., Jongejan J.A., De Vries S., Duine J.A.
    Eur. J. Biochem. 230:899-905(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 32-54 AND 477-490.
    Strain: ATCC 15667 / JCM 13048 / LMG 7106 / NCIB 9682.
  3. "Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni."
    Groen B.W., van Kleef M.A., Duine J.A.
    Biochem. J. 234:611-615(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. "Crystallization of quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni: crystals with unique optical properties."
    Oubrie A., Huizinga E.G., Rozeboom H.J., Kalk K.H., de Jong G.A.H., Duine J.A., Dijkstra B.W.
    Acta Crystallogr. D 57:1732-1734(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  5. "Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer."
    Oubrie A., Rozeboom H.J., Kalk K.H., Huizinga E.G., Dijkstra B.W.
    J. Biol. Chem. 277:3727-3732(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS).

Entry informationi

Entry nameiQHED_COMTE
AccessioniPrimary (citable) accession number: Q46444
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

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

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.