Quinohemoprotein alcohol dehydrogenase ADH IIB
Details
- Name
- Quinohemoprotein alcohol dehydrogenase ADH IIB
- Synonyms
- 1.1.9.1
- ADH IIB
- Alcohol dehydrogenase (azurin)
- Gene Name
- qbdA
- Organism
- Pseudomonas putida
- Amino acid sequence
>lcl|BSEQ0016929|Quinohemoprotein alcohol dehydrogenase ADH IIB MKKPLRTSLLMLCLATPLAALAAGVDEAAIRATEQAGGEWLSHGRTYAEQRFSPLKQIDA SNVRSLGLAWYMDLDNTRGLEATPLFHDGVIYTSMSWSRVIAVDAASGKELWRYDPEVAK VKARTSCCDAVNRGVALWGDKVYVGTLDGRLIALDAKTGKAIWSQQTTDPAKPYSITGAP RVVKGKVIIGNGGAEYGVRGFVSAYDADTGKLAWRFYTVPGDPALPYEHPELREAAKTWQ GDQYWKLGGGGTVWDSMAYDPELDLLYVGTGNGSPWNREVRSPGGGDNLYLSSILAIRPD TGKLAWHYQVTPGDSWDFTATQQITLAELNIDGKPRKVLMQAPKNGFFYVLDRTNGKLIS AEKFGKVTWAEKVDLATGRPVEAPGVRYEKEPIVMWPSPFGAHNWHSMSFNPGTGLVYIP YQEVPGVYRNEGKDFVTRKAFNTAAGFADATDVPAAVVSGALLAWDPVKQKAAWKVPYPT HWNGGTLSTAGNLVFQGTAAGQMHAYSADKGEALWQFEAQSGIVAAPMTFELAGRQYVAI MAGWGGVATLTGGESMNLPGMKNRSRLLVFALDGKAQLPPPAPAPAKVERVPQPVTAAPE QVQAGKQLYGQFCSVCHGMGTISGGLIPDLRQSSDATREHFQQIVLQGALKPLGMPSFDD SLKPEEVEQIKLYVMSREYEDYMARHKAAP
- Number of residues
- 690
- Molecular Weight
- 74968.745
- Theoretical pI
- 7.62
- GO Classification
- Functionscalcium ion binding / electron carrier activity / heme binding / metal ion binding / oxidoreductase activity / oxidoreductase activity, acting on CH-OH group of donors / pyrroloquinoline quinone bindingComponentsmembrane / outer membrane-bounded periplasmic space
- General Function
- Pyrroloquinoline quinone binding
- Specific Function
- Catalyzes the dye-linked oxidation of primary alcohols to the corresponding aldehydes and the (subsequent) oxidation of the aldehydes to carboxylic acids. Exhibits activity with longer mono-alcohols (C-4 to C-7) but not with methanol or glycerol. Reacts with 1,2-propanediol and 1,3-propanediol but not with sugar alcohols such as D-sorbitol.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Periplasm
- Gene sequence
>lcl|BSEQ0005688|2073 bp ATGAAAAAACCTTTGCGTACTTCATTGCTGATGCTGTGCCTGGCCACCCCGCTGGCAGCC CTTGCCGCCGGGGTGGACGAGGCCGCCATCCGCGCCACCGAACAGGCCGGCGGCGAGTGG CTCAGCCACGGCCGCACCTATGCCGAACAACGCTTCAGCCCGCTCAAACAGATCGACGCC AGCAACGTCAGGTCACTGGGCCTGGCCTGGTACATGGACCTGGACAACACCCGCGGCCTG GAGGCGACACCGCTGTTCCACGACGGGGTGATCTACACCTCGATGTCCTGGAGCCGGGTG ATCGCGGTCGACGCCGCCAGCGGCAAGGAGCTGTGGCGCTACGACCCCGAGGTGGCCAAG GTCAAGGCCCGTACCTCGTGCTGCGACGCGGTCAACCGCGGCGTGGCACTCTGGGGCGAC AAGGTCTACGTCGGCACCCTGGACGGGCGTCTGATCGCCCTCGACGCCAAGACCGGCAAG GCCATCTGGAGCCAGCAGACCACCGACCCGGCCAAGCCCTACAGCATCACCGGCGCGCCA CGGGTGGTCAAAGGCAAGGTCATCATCGGCAACGGCGGCGCCGAATACGGCGTGCGCGGC TTCGTCTCGGCCTATGACGCCGACACCGGCAAACTGGCCTGGCGCTTCTACACCGTACCG GGCGACCCGGCGCTGCCCTACGAGCACCCCGAACTGCGCGAAGCGGCCAAGACCTGGCAG GGCGACCAGTACTGGAAGCTCGGCGGTGGCGGCACGGTGTGGGACAGCATGGCCTACGAC CCCGAGCTGGACCTGCTCTACGTCGGCACCGGCAACGGCTCGCCGTGGAACCGCGAGGTG CGCAGCCCGGGCGGTGGCGACAACCTGTACCTGTCGTCGATCCTCGCCATCCGCCCCGAC ACCGGCAAGCTGGCCTGGCACTACCAGGTCACCCCGGGCGACAGCTGGGACTTCACCGCC ACCCAGCAGATCACCCTGGCCGAGCTGAACATCGACGGCAAACCGCGCAAGGTCCTGATG CAGGCGCCTAAAAACGGCTTCTTCTACGTGCTCGACCGCACCAACGGCAAGCTGATCTCG GCCGAGAAGTTCGGCAAGGTCACCTGGGCCGAGAAGGTCGACCTCGCCACCGGCCGGCCG GTCGAGGCCCCTGGGGTGCGCTACGAAAAAGAGCCCATCGTGATGTGGCCCAGCCCCTTC GGCGCGCACAACTGGCATTCGATGTCGTTCAACCCCGGCACCGGCCTGGTGTACATCCCC TACCAGGAAGTGCCCGGTGTGTACCGCAACGAAGGCAAGGACTTCGTTACCCGCAAGGCA TTCAACACCGCCGCCGGCTTTGCCGACGCCACCGACGTGCCGGCCGCCGTGGTCAGCGGC GCCTTGCTGGCCTGGGACCCGGTCAAGCAGAAGGCCGCCTGGAAGGTGCCGTACCCCACG CACTGGAACGGCGGCACCCTGAGCACCGCCGGCAACCTGGTGTTCCAGGGCACTGCGGCG GGGCAGATGCATGCCTATTCCGCCGACAAGGGCGAGGCGCTGTGGCAGTTCGAGGCGCAA AGCGGCATCGTTGCCGCGCCCATGACCTTCGAACTGGCCGGGCGTCAGTACGTGGCGATC ATGGCCGGCTGGGGCGGCGTGGCCACCCTGACCGGCGGCGAGTCGATGAACCTGCCGGGC ATGAAGAACCGCAGCCGCCTGCTGGTGTTCGCCCTCGATGGCAAGGCGCAGTTGCCGCCA CCGGCCCCGGCGCCCGCCAAGGTCGAGCGCGTGCCCCAGCCCGTCACCGCAGCACCCGAG CAGGTGCAGGCCGGCAAGCAGCTGTATGGCCAGTTCTGCAGCGTGTGCCACGGCATGGGC ACCATCAGCGGCGGTTTGATTCCCGACCTGCGCCAGTCCAGCGACGCCACCCGCGAGCAC TTCCAGCAGATCGTCCTGCAGGGCGCGCTCAAGCCACTGGGCATGCCGTCGTTCGACGAC TCGCTCAAGCCCGAGGAGGTCGAGCAGATCAAGCTCTACGTGATGTCGCGCGAGTACGAG GACTACATGGCGCGGCACAAAGCCGCACCCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q8GR64 UniProtKB Entry Name QHED_PSEPU GenBank Gene ID AB091400 - General References
- Toyama H, Fujii T, Aoki N, Matsushita K, Adachi O: Molecular cloning of quinohemoprotein alcohol dehydrogenase, ADH IIB, from Pseudomonas putida HK5. Biosci Biotechnol Biochem. 2003 Jun;67(6):1397-400. [Article]
- Toyama H, Fujii A, Matsushita K, Shinagawa E, Ameyama M, Adachi O: Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols. J Bacteriol. 1995 May;177(9):2442-50. [Article]
- Matsushita K, Yamashita T, Aoki N, Toyama H, Adachi O: Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory chain of Pseudomonas putida HK5. Biochemistry. 1999 May 11;38(19):6111-8. [Article]
- Toyama H, Chen ZW, Fukumoto M, Adachi O, Matsushita K, Mathews FS: Molecular cloning and structural analysis of quinohemoprotein alcohol dehydrogenase ADH-IIG from Pseudomonas putida HK5. J Mol Biol. 2005 Sep 9;352(1):91-104. [Article]
- Promden W, Vangnai AS, Pongsawasdi P, Adachi O, Matsushita K, Toyama H: Disruption of quinoprotein ethanol dehydrogenase gene and adjacent genes in Pseudomonas putida HK5. FEMS Microbiol Lett. 2008 Mar;280(2):203-9. doi: 10.1111/j.1574-6968.2008.01060.x. Epub 2008 Jan 19. [Article]
- Promden W, Vangnai AS, Toyama H, Matsushita K, Pongsawasdi P: Analysis of the promoter activities of the genes encoding three quinoprotein alcohol dehydrogenases in Pseudomonas putida HK5. Microbiology. 2009 Feb;155(Pt 2):594-603. doi: 10.1099/mic.0.021956-0. [Article]
- Chen Z, Baruch P, Mathews FS, Matsushita K, Yamashita T, Toyama H, Adachi O: Crystallization and preliminary diffraction studies of two quinoprotein alcohol dehydrogenases (ADHs): a soluble monomeric ADH from Pseudomonas putida HK5 (ADH-IIB) and a heterotrimeric membrane-bound ADH from Gluconobacter suboxydans (ADH-GS). Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1933-6. [Article]
- Chen ZW, Matsushita K, Yamashita T, Fujii TA, Toyama H, Adachi O, Bellamy HD, Mathews FS: Structure at 1.9 A resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5. Structure. 2002 Jun;10(6):837-49. [Article]