2,5-diketo-D-gluconic acid reductase A
Details
- Name
- 2,5-diketo-D-gluconic acid reductase A
- Synonyms
- 1.1.1.346
- 2,5-DKG reductase A
- AKR5C
- Gene Name
- dkgA
- Organism
- Corynebacterium sp. (strain ATCC 31090)
- Amino acid sequence
>lcl|BSEQ0022011|2,5-diketo-D-gluconic acid reductase A MTVPSIVLNDGNSIPQLGYGVFKVPPADTQRAVEEALEVGYRHIDTAAIYGNEEGVGAAI AASGIARDDLFITTKLWNDRHDGDEPAAAIAESLAKLALDQVDLYLVHWPTPAADNYVHA WEKMIELRAAGLTRSIGVSNHLVPHLERIVAATGVVPAVNQIELHPAYQQREITDWAAAH DVKIESWGPLGQGKYDLFGAEPVTAAAAAHGKTPAQAVLRWHLQKGFVVFPKSVRRERLE ENLDVFDFDLTDTEIAAIDAMDPGDGSGRVSAHPDEVD
- Number of residues
- 278
- Molecular Weight
- 30118.485
- Theoretical pI
- 4.56
- GO Classification
- Functionsoxidoreductase activityProcessesL-ascorbic acid biosynthetic processComponentscytoplasm
- General Function
- Oxidoreductase activity
- Specific Function
- Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates. 25DKGR-A exhibits a greater selectivity for the substrate and higher thermal stability than 25DKGR-B.
- Pfam Domain Function
- Aldo_ket_red (PF00248)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0005134|837 bp ATGACAGTTCCCAGCATCGTGCTCAACGACGGCAATTCCATTCCCCAGCTCGGGTACGGC GTCTTCAAGGTGCCGCCGGCGGACACCCAGCGCGCCGTCGAGGAAGCGCTCGAAGTCGGC TACCGGCACATCGACACCGCGGCGATCTACGGAAACGAAGAAGGCGTCGGCGCCGCGATC GCGGCGAGCGGCATCGCGCGCGACGACCTGTTCATCACGACGAAGCTCTGGAACGATCGC CACGACGGCGATGAGCCCGCTGCAGCGATCGCCGAGAGCCTCGCGAAGCTGGCACTCGAT CAGGTCGACCTGTACCTCGTGCACTGGCCGACGCCCGCCGCCGACAACTACGTGCACGCG TGGGAGAAGATGATCGAGCTTCGCGCAGCCGGTCTCACCCGCAGCATCGGCGTCTCGAAC CACCTCGTGCCGCACCTCGAGCGCATCGTCGCCGCCACCGGCGTCGTGCCGGCGGTGAAC CAGATCGAGCTGCACCCCGCCTACCAGCAGCGCGAGATCACCGACTGGGCCGCCGCCCAC GACGTGAAGATCGAATCGTGGGGGCCGCTCGGTCAGGGCAAGTACGACCTCTTCGGCGCC GAGCCCGTCACTGCGGCTGCCGCCGCCCACGGCAAGACCCCGGCGCAGGCCGTGCTCCGT TGGCACCTGCAGAAGGGTTTCGTGGTCTTCCCGAAGTCGGTCCGCCGCGAGCGCCTCGAA GAGAACCTCGACGTGTTCGACTTCGACCTCACCGACACCGAGATCGCCGCGATCGACGCG ATGGATCCGGGCGACGGTTCGGGTCGCGTGAGCGCACACCCCGATGAGGTCGACTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P06632 UniProtKB Entry Name DKGA_CORSC GenBank Gene ID M12799 - General References
- Miller JV, Estell DA, Lazarus RA: Purification and characterization of 2,5-diketo-D-gluconate reductase from Corynebacterium sp. J Biol Chem. 1987 Jul 5;262(19):9016-20. [Article]
- Khurana S, Sanli G, Powers DB, Anderson S, Blaber M: Molecular modeling of substrate binding in wild-type and mutant Corynebacteria 2,5-diketo-D-gluconate reductases. Proteins. 2000 Apr 1;39(1):68-75. [Article]
- Khurana S, Powers DB, Anderson S, Blaber M: Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-A resolution. Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6768-73. [Article]
- Sanli G, Blaber M: Structural assembly of the active site in an aldo-keto reductase by NADPH cofactor. J Mol Biol. 2001 Jun 22;309(5):1209-18. [Article]
- Sanli G, Banta S, Anderson S, Blaber M: Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase. Protein Sci. 2004 Feb;13(2):504-12. Epub 2004 Jan 10. [Article]