Quinohemoprotein ethanol dehydrogenase type-1

Details

Name
Quinohemoprotein ethanol dehydrogenase type-1
Synonyms
  • 1.1.9.1
  • Alcohol dehydrogenase (azurin)
  • QH-EDH1
  • Quinohemoprotein ethanol dehydrogenase type I
Gene Name
qheDH
Organism
Comamonas testosteroni
Amino acid sequence
>lcl|BSEQ0019194|Quinohemoprotein ethanol dehydrogenase type-1
MERLIDNSHGWPGRMVWLLAACLGSAAAFAQTGPAAQAAAAVQRVDGDFIRANAARTPDW
PTIGVDYAETRYSRLDQINAANVKDLGLAWSYNLESTRGVEATPVVVDGIMYVSASWSVV
HAIDTRTGNRIWTYDPQIDRSTGFKGCCDVVNRGVALWKGKVYVGAWDGRLIALDAATGK
EVWHQNTFEGQKGSLTITGAPRVFKGKVIIGKRGAEYGVRGYITAYDAETGERKWRWFSV
PGDPSKPFEDESMKRAARTWDPSGKWWEAGGGGTMWDSMTFDAELNTMYVGTGNGSPWSH
KVRSPKGGDNLYLASIVALDPDTGKYKWHYQETPGDNWDYTSTQPMILADIKIAGKPRKV
ILHAPKNGFFFVLDRTNGKFISAKNFVPVNWASGYDKHGKPIGIAAARDGSKPQDAVPGP
YGAHNWHPMSFNPQTGLVYLPAQNVPVNLMDDKKWEFNQAGPGKPQSGTGWNTAKFFNAE
PPKSKPFGRLLAWDPVAQKAAWSVEHVSPWNGGTLTTAGNVVFQGTADGRLVAYHAATGE
KLWEAPTGTGVVAAPSTYMVDGRQYVSVAVGWGGVYGLAARATERQGPGTVYTFVVAGKA
RMPEFVAQRTGQLLQGVKYDPAKVEAGTMLYVANCVFCHGVPGVDRGGNIPNLGYMDASY
IENLPNFVFKGPAMVRGMPDFTGKLSGDDVESLKAFIQGTADAIRPKP
Number of residues
708
Molecular Weight
76822.435
Theoretical pI
9.21
GO Classification
Functions
calcium ion binding / electron carrier activity / heme binding / oxidoreductase activity, acting on CH-OH group of donors
Components
membrane / outer membrane-bounded periplasmic space
General Function
Oxidoreductase activity, acting on ch-oh group of donors
Specific Function
Catalyzes the dye-linked oxidation of primary alcohols to the corresponding aldehydes and the (subsequent) oxidation of the aldehydes to carboxylic acids.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0003704|2127 bp
ATGGAACGGCTGATCGACAACTCTCATGGATGGCCGGGCCGCATGGTCTGGCTGCTGGCC
GCCTGCCTGGGCAGCGCAGCGGCTTTCGCGCAAACCGGCCCTGCAGCGCAGGCTGCTGCT
GCCGTGCAGCGCGTCGACGGCGATTTCATCCGCGCCAATGCCGCCAGGACGCCTGACTGG
CCCACCATCGGCGTGGACTATGCCGAGACCCGCTACAGCCGCCTCGATCAGATCAATGCC
GCCAACGTCAAGGACCTGGGCCTGGCATGGTCGTACAACCTCGAGTCCACGCGCGGCGTG
GAGGCCACGCCTGTCGTGGTGGACGGCATCATGTATGTCAGCGCCTCATGGAGCGTGGTG
CATGCCATCGACACCCGTACCGGCAACAGGATCTGGACCTATGACCCGCAGATCGACCGC
AGCACCGGCTTCAAGGGGTGCTGCGACGTCGTCAACCGCGGCGTGGCGCTGTGGAAGGGC
AAGGTCTATGTGGGGGCGTGGGATGGCCGCCTGATCGCGCTGGATGCCGCCACCGGCAAG
GAGGTCTGGCACCAAAATACCTTCGAGGGGCAGAAGGGGTCGCTCACCATCACCGGCGCC
CCGCGCGTGTTCAAGGGCAAGGTCATCATCGGCAAACGCGGCGCCGAATATGGCGTGCGC
GGCTATATCACTGCCTATGACGCCGAGACCGGGGAGCGGAAATGGCGCTGGTTCAGCGTA
CCCGGCGATCCCTCCAAACCCTTCGAGGACGAGTCCATGAAGCGCGCCGCCAGGACCTGG
GACCCCAGCGGCAAATGGTGGGAGGCCGGCGGCGGCGGCACCATGTGGGACAGCATGACC
TTCGATGCCGAACTCAACACCATGTACGTGGGCACGGGCAATGGATCGCCCTGGTCGCAC
AAGGTGCGCAGCCCCAAGGGCGGCGACAACCTGTACCTGGCCTCCATCGTGGCCCTGGAT
CCCGACACCGGCAAATACAAGTGGCACTATCAGGAAACACCGGGCGACAACTGGGACTAC
ACCTCCACCCAGCCCATGATCCTGGCCGACATCAAGATCGCCGGCAAGCCGCGCAAGGTC
ATACTGCATGCGCCCAAGAACGGCTTCTTCTTCGTGCTCGACCGCACCAATGGAAAGTTC
ATCTCGGCCAAGAACTTCGTGCCCGTGAACTGGGCCAGCGGCTACGACAAGCACGGCAAG
CCCATCGGCATTGCCGCAGCGCGCGACGGCAGCAAGCCCCAGGACGCGGTGCCGGGCCCC
TATGGCGCGCACAACTGGCACCCCATGTCCTTCAACCCCCAGACGGGCCTGGTGTATCTG
CCTGCGCAGAACGTGCCCGTCAACCTGATGGACGACAAGAAATGGGAGTTCAACCAGGCC
GGACCGGGCAAGCCCCAGTCGGGCACCGGCTGGAACACGGCCAAGTTCTTCAATGCCGAG
CCGCCCAAGAGCAAGCCCTTTGGTCGTCTGCTGGCCTGGGACCCCGTTGCGCAAAAGGCC
GCCTGGAGCGTGGAGCATGTCTCGCCCTGGAACGGCGGCACGCTGACCACGGCGGGCAAT
GTGGTGTTCCAGGGAACGGCTGATGGCCGCCTCGTGGCCTATCACGCGGCCACGGGCGAG
AAACTGTGGGAAGCGCCCACGGGCACCGGTGTGGTGGCCGCGCCCAGCACCTATATGGTG
GACGGCAGGCAGTATGTCTCGGTGGCCGTGGGCTGGGGCGGTGTCTACGGTCTGGCTGCG
CGCGCCACCGAGCGCCAGGGCCCGGGCACGGTCTATACCTTCGTCGTGGCCGGCAAGGCC
AGGATGCCGGAGTTCGTGGCCCAGCGCACCGGCCAGTTGCTGCAGGGCGTGAAATACGAC
CCCGCCAAGGTCGAGGCCGGCACCATGCTGTATGTGGCCAACTGCGTTTTCTGTCACGGC
GTGCCTGGCGTGGACCGTGGCGGAAACATTCCCAATCTGGGTTACATGGACGCGAGCTAT
ATCGAGAACCTGCCAAACTTTGTCTTCAAGGGCCCGGCCATGGTGCGCGGCATGCCGGAC
TTCACGGGCAAGTTGTCGGGCGATGACGTGGAGTCCCTCAAGGCCTTCATCCAGGGCACG
GCGGACGCCATCCGGCCCAAGCCCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ46444
UniProtKB Entry NameQHED_COMTE
GenBank Protein ID663196
GenBank Gene IDX81880
General References
  1. Stoorvogel J, Kraayveld DE, Van Sluis CA, Jongejan JA, De Vries S, Duine JA: Characterization of the gene encoding quinohaemoprotein ethanol dehydrogenase of Comamonas testosteroni. Eur J Biochem. 1996 Feb 1;235(3):690-8. [PubMed:8654419]
  2. de Jong GA, Geerlof A, Stoorvogel J, Jongejan JA, de Vries S, Duine JA: Quinohaemoprotein ethanol dehydrogenase from Comamonas testosteroni. Purification, characterization, and reconstitution of the apoenzyme with pyrroloquinoline quinone analogues. Eur J Biochem. 1995 Jun 15;230(3):899-905. [PubMed:7601151]
  3. Groen BW, van Kleef MA, Duine JA: Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni. Biochem J. 1986 Mar 15;234(3):611-5. [PubMed:3521592]
  4. Oubrie A, Huizinga EG, Rozeboom HJ, Kalk KH, de Jong GA, Duine JA, Dijkstra BW: Crystallization of quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni: crystals with unique optical properties. Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1732-4. Epub 2001 Oct 25. [PubMed:11679760]
  5. Oubrie A, Rozeboom HJ, Kalk KH, Huizinga EG, Dijkstra BW: Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer. J Biol Chem. 2002 Feb 1;277(5):3727-32. Epub 2001 Nov 19. [PubMed:11714714]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03051Tetrahydrofuran-2-Carboxylic AcidexperimentalunknownDetails
DB03205Pyrroloquinoline QuinoneexperimentalunknownDetails
DB03317Heme CexperimentalunknownDetails
DB036792-Hydroxy-TryptophanexperimentalunknownDetails