UniProtKB - Q46444 (QHED_COMTE)
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>sp|Q46444|QHED_COMTE Quinohemoprotein alcohol dehydrogenase OS=Comamonas testosteroni OX=285 GN=qheDH PE=1 SV=1 MERLIDNSHGWPGRMVWLLAACLGSAAAFAQTGPAAQAAAAVQRVDGDFIRANAARTPDW PTIGVDYAETRYSRLDQINAANVKDLGLAWSYNLESTRGVEATPVVVDGIMYVSASWSVV HAIDTRTGNRIWTYDPQIDRSTGFKGCCDVVNRGVALWKGKVYVGAWDGRLIALDAATGK EVWHQNTFEGQKGSLTITGAPRVFKGKVIIGKRGAEYGVRGYITAYDAETGERKWRWFSV PGDPSKPFEDESMKRAARTWDPSGKWWEAGGGGTMWDSMTFDAELNTMYVGTGNGSPWSH KVRSPKGGDNLYLASIVALDPDTGKYKWHYQETPGDNWDYTSTQPMILADIKIAGKPRKV ILHAPKNGFFFVLDRTNGKFISAKNFVPVNWASGYDKHGKPIGIAAARDGSKPQDAVPGP YGAHNWHPMSFNPQTGLVYLPAQNVPVNLMDDKKWEFNQAGPGKPQSGTGWNTAKFFNAE PPKSKPFGRLLAWDPVAQKAAWSVEHVSPWNGGTLTTAGNVVFQGTADGRLVAYHAATGE KLWEAPTGTGVVAAPSTYMVDGRQYVSVAVGWGGVYGLAARATERQGPGTVYTFVVAGKA RMPEFVAQRTGQLLQGVKYDPAKVEAGTMLYVANCVFCHGVPGVDRGGNIPNLGYMDASY IENLPNFVFKGPAMVRGMPDFTGKLSGDDVESLKAFIQGTADAIRPKPCommunity curation ()Add a publicationFeedback
Quinohemoprotein alcohol dehydrogenase
qheDH
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.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]
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
Caution
Manual assertion inferred by curator fromi
- Ref.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) IN COMPLEX WITH HEME C, PYRROLOQUINOLINE QUINONE AND CALCIUM IONS, COFACTOR, ACTIVE SITE, DISULFIDE BOND, REACTION MECHANISM.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- a primary alcoholEC:1.1.9.1
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- See the description of this molecule in ChEBI.
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- See the description of this molecule in ChEBI.
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- See the description of this molecule in ChEBI.
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Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
- Search proteins in UniProtKB for this EC number.
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Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
a primary alcohol- Search proteins in UniProtKB for this molecule.
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+2oxidized [azurin]- Search proteins in UniProtKB for this molecule.
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Cu2+zoom- Search proteins in UniProtKB for this molecule.
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=an aldehyde- Search proteins in UniProtKB for this molecule.
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+2H+- Search proteins in UniProtKB for this molecule.
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+2reduced [azurin]- Search proteins in UniProtKB for this molecule.
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Cu+- Search proteins in UniProtKB for this molecule.
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<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Protein has several cofactor binding sites:- pyrroloquinoline quinone
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Manual assertion inferred by curator fromi
- Ref.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], PROTEIN SEQUENCE OF 32-54, COFACTOR. - Ref.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]
Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.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) IN COMPLEX WITH HEME C, PYRROLOQUINOLINE QUINONE AND CALCIUM IONS, COFACTOR, ACTIVE SITE, DISULFIDE BOND, REACTION MECHANISM.
Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.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) IN COMPLEX WITH HEME C, PYRROLOQUINOLINE QUINONE AND CALCIUM IONS, COFACTOR, ACTIVE SITE, DISULFIDE BOND, REACTION MECHANISM.
- Ca2+
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion inferred by curator fromi
- Ref.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], PROTEIN SEQUENCE OF 32-54, COFACTOR. - Ref.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]
Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.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) IN COMPLEX WITH HEME C, PYRROLOQUINOLINE QUINONE AND CALCIUM IONS, COFACTOR, ACTIVE SITE, DISULFIDE BOND, REACTION MECHANISM.
Manual assertion based on experiment ini
- Ref.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) IN COMPLEX WITH HEME C, PYRROLOQUINOLINE QUINONE AND CALCIUM IONS, COFACTOR, ACTIVE SITE, DISULFIDE BOND, REACTION MECHANISM.
- heme c
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion inferred by curator fromi
- Ref.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], PROTEIN SEQUENCE OF 32-54, COFACTOR. - Ref.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]
Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.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) IN COMPLEX WITH HEME C, PYRROLOQUINOLINE QUINONE AND CALCIUM IONS, COFACTOR, ACTIVE SITE, DISULFIDE BOND, REACTION MECHANISM.
Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.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) IN COMPLEX WITH HEME C, PYRROLOQUINOLINE QUINONE AND CALCIUM IONS, COFACTOR, ACTIVE SITE, DISULFIDE BOND, REACTION MECHANISM.
<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=5 µM for benzyl alcohol1 Publication
Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
- KM=5 µM for butan-1-ol1 Publication
Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
- KM=5 µM for pentan-1-ol1 Publication
Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
- KM=5 µM for octan-1-ol1 Publication
Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
- KM=40 µM for octanal1 Publication
Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
- KM=60 µM for propan-1-ol1 Publication
Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
- KM=100 µM for butyraldehyde1 Publication
Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
- KM=200 µM for 6-aminohexan-1-ol1 Publication
Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
- KM=280 µM for butan-1,3-diol1 Publication
Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
- KM=900 µM for acetaldehyde1 Publication
Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
- KM=3 mM for formaldehyde1 Publication
Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
- KM=5 mM for ethanol1 Publication
Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
pH dependencei
Manual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 101 | Pyrroloquinoline quinoneCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Binding sitei | 153 | Pyrroloquinoline quinoneCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Binding sitei | 198 | Pyrroloquinoline quinoneCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 216 | CalciumCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Binding sitei | 274 | Pyrroloquinoline quinoneCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Metal bindingi | 294 | CalciumCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 339 | Proton acceptor1 Publication Manual assertion inferred by curator fromi
| 1 | |
Metal bindingi | 339 | CalciumCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Binding sitei | 366 | Pyrroloquinoline quinoneCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Binding sitei | 575 | Pyrroloquinoline quinone; via amide nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Binding sitei | 635 | Heme c; covalentCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Binding sitei | 638 | Heme c; covalentCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Metal bindingi | 639 | Iron (heme axial ligand); via tele nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Metal bindingi | 678 | Iron (heme axial ligand)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- calcium ion binding Source: InterPro
- electron transfer activity Source: InterPro
- heme binding Source: InterPro
- oxidoreductase activity, acting on CH-OH group of donors Source: InterPro
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
Molecular function | Oxidoreductase |
Ligand | Calcium, Heme, Iron, Metal-binding, PQQ |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.1.9.1, 1590 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Quinohemoprotein alcohol dehydrogenase1 Publication<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Manual assertion based on experiment ini
Short name: QH-ADH1 Publication Manual assertion based on opinion ini
Alternative name(s): Alcohol dehydrogenase (azurin)Curated PQQ-containing alcohol dehydrogenase1 Publication Manual assertion based on opinion ini
PQQ-dependent ADH1 Publication Manual assertion based on opinion ini
Quinohaemoprotein ethanol dehydrogenase type I1 Publication Manual assertion based on opinion ini
Short name: QH-EDHI1 Publication Manual assertion based on opinion ini
|
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:qheDH1 Publication Manual assertion based on opinion ini
|
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Comamonas testosteroni (Pseudomonas testosteroni) |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 285 [NCBI] |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Comamonas |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Other locations
- Periplasm 1 Publication
Manual assertion inferred by curator fromi
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
- Periplasm 1 Publication
Other locations
- membrane Source: InterPro
- outer membrane-bounded periplasmic space Source: InterPro
Keywords - Cellular componenti
Periplasm<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Chemistry databases
Drug and drug target database More...DrugBanki | DB03051, (S)-2-Tetrahydrofuroic acid DB03679, 2-Hydroxy-Tryptophan DB03317, Ferroheme C DB03205, Pyrroloquinoline Quinone |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 31 | 2 Publications Manual assertion based on experiment ini
| 31 | |
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000025563 | 32 – 708 | Quinohemoprotein alcohol dehydrogenaseAdd BLAST | 677 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 147 ↔ 148 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
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<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Manual assertion based on experiment ini
- Ref.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) IN COMPLEX WITH HEME C, PYRROLOQUINOLINE QUINONE AND CALCIUM IONS, COFACTOR, ACTIVE SITE, DISULFIDE BOND, REACTION MECHANISM.
Keywords - PTMi
Disulfide bond<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
Manual assertion inferred by curator fromi
- Ref.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], PROTEIN SEQUENCE OF 32-54, COFACTOR.
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Monomer.
1 PublicationManual assertion based on experiment ini
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 33 – 43 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
Helixi | 47 – 52 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 53 – 55 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 80 – 82 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 83 – 85 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 86 – 93 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 105 – 107 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 110 – 114 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 116 – 118 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 120 – 124 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Turni | 125 – 127 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 130 – 134 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 140 – 145 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 146 – 148 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 156 – 158 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 161 – 165 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 169 – 175 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Turni | 176 – 178 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 181 – 186 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Turni | 187 – 190 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 202 – 204 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 207 – 210 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 215 – 217 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 222 – 227 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Turni | 228 – 230 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 233 – 240 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 251 – 257 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 262 – 264 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 266 – 269 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 279 – 282 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 283 – 286 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 287 – 291 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 295 – 298 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 300 – 303 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 311 – 314 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 315 – 319 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Turni | 321 – 323 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 326 – 333 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 347 – 353 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 356 – 363 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 368 – 374 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Turni | 375 – 377 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 380 – 387 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 390 – 395 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 401 – 403 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 405 – 408 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 430 – 432 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 433 – 436 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 437 – 444 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 448 – 451 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 467 – 469 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 475 – 477 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 487 – 494 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Turni | 495 – 498 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 499 – 509 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
Beta strandi | 514 – 517 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 518 – 520 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 521 – 525 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 529 – 535 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Turni | 536 – 538 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 541 – 546 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 556 – 560 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 563 – 570 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 574 – 579 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 590 – 596 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 621 – 623 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 624 – 634 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
Helixi | 636 – 639 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 642 – 644 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 648 – 650 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 653 – 655 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 658 – 662 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 664 – 668 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 674 – 676 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 682 – 684 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 689 – 704 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 16 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q46444 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q46444 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 619 – 708 | Cytochrome cPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 90 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 214 – 215 | Pyrroloquinoline quinone bindingCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 2 | |
Regioni | 425 – 426 | Pyrroloquinoline quinone bindingCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 2 |
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Keywords - Domaini
SignalFamily and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.760.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View 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 |
Pfam protein domain database More...Pfami | View protein in Pfam PF13442, Cytochrome_CBB3, 1 hit PF13360, PQQ_2, 2 hits |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00564, PQQ, 5 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF46626, SSF46626, 1 hit SSF50998, SSF50998, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR03075, PQQ_enz_alc_DH, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00364, BACTERIAL_PQQ_2, 1 hit PS51007, CYTC, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
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
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X81880 Genomic DNA Translation: CAA57464.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S62366, S52317 |
Genome annotation databases
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ag:CAA57464 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
Q46444 | PQQ-dependent dehydrogenase, methanol/ethanol family | 709 | UniRef90_Q46444 | |||
PQQ-dependent dehydrogenase, methanol/ethanol family | 708 | |||||
PQQ-dependent dehydrogenase, methanol/ethanol family | 708 | |||||
PQQ-dependent dehydrogenase, methanol/ethanol family | 708 | |||||
Quino(Hemo)protein alcohol dehydrogenase | 708 | |||||
+27 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
Q46444 | 1-butanol dehydrogenase (cytochrome c) | 691 | UniRef50_Q46444 | |||
PQQ-dependent dehydrogenase, methanol/ethanol family | 709 | |||||
Quino(Hemo)protein alcohol dehydrogenase | 708 | |||||
Alcohol dehydrogenase | 708 | |||||
PQQ-dependent dehydrogenase, methanol/ethanol family | 708 | |||||
+608 |
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X81880 Genomic DNA Translation: CAA57464.1 |
PIRi | S62366, S52317 |
3D structure databases
Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1KB0 | X-ray | 1.44 | A | 32-708 | [»] | |
SMRi | Q46444 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Chemistry databases
DrugBanki | DB03051, (S)-2-Tetrahydrofuroic acid DB03679, 2-Hydroxy-Tryptophan DB03317, Ferroheme C DB03205, Pyrroloquinoline Quinone |
Genome annotation databases
KEGGi | ag:CAA57464 |
Enzyme and pathway databases
BRENDAi | 1.1.9.1, 1590 |
Miscellaneous databases
EvolutionaryTracei | Q46444 |
Family and domain databases
Gene3Di | 1.10.760.10, 1 hit |
InterProi | View 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 |
Pfami | View protein in Pfam PF13442, Cytochrome_CBB3, 1 hit PF13360, PQQ_2, 2 hits |
SMARTi | View protein in SMART SM00564, PQQ, 5 hits |
SUPFAMi | SSF46626, SSF46626, 1 hit SSF50998, SSF50998, 1 hit |
TIGRFAMsi | TIGR03075, PQQ_enz_alc_DH, 1 hit |
PROSITEi | View protein in PROSITE PS00364, BACTERIAL_PQQ_2, 1 hit PS51007, CYTC, 1 hit |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | QHED_COMTE | |
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q46444Primary (citable) accession number: Q46444 | |
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 17, 2003 |
Last sequence update: | November 1, 1996 | |
Last modified: | February 23, 2022 | |
This is version 135 of the entry and version 1 of the sequence. See complete history. | ||
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families