3-keto-L-gulonate-6-phosphate decarboxylase UlaD
Details
- Name
- 3-keto-L-gulonate-6-phosphate decarboxylase UlaD
- Synonyms
- 3-dehydro-L-gulonate-6-phosphate decarboxylase
- 4.1.1.85
- KGPDC
- L-ascorbate utilization protein D
- sgaH
- yjfV
- Gene Name
- ulaD
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0010871|3-keto-L-gulonate-6-phosphate decarboxylase UlaD MSLPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALYPHKIVL ADAKIADAGKILSRMCFEANADWVTVICCADINTAKGALDVAKEFNGDVQIELTGYWTWE QAQQWRDAGIGQVVYHRSRDAQAAGVAWGEADITAIKRLSDMGFKVTVTGGLALEDLPLF KGIPIHVFIAGRSIRDAASPVEAARQFKRSIAELWG
- Number of residues
- 216
- Molecular Weight
- 23577.835
- Theoretical pI
- 4.79
- GO Classification
- Functions3-dehydro-L-gulonate-6-phosphate decarboxylase activity / magnesium ion binding / orotidine-5'-phosphate decarboxylase activityProcesses'de novo' pyrimidine nucleobase biosynthetic process / L-ascorbic acid catabolic process
- General Function
- Orotidine-5'-phosphate decarboxylase activity
- Specific Function
- Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. Is involved in the anaerobic L-ascorbate utilization.
- Pfam Domain Function
- OMPdecase (PF00215)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0010872|3-keto-L-gulonate-6-phosphate decarboxylase UlaD (ulaD) ATGTCATTACCGATGTTGCAAGTCGCGCTGGACAACCAGACTATGGATAGCGCCTACGAA ACCACTCGCCTGATTGCCGAAGAAGTCGACATTATCGAAGTGGGCACCATTCTGTGCGTG GGCGAAGGCGTGCGTGCGGTTCGTGACCTGAAAGCGCTCTACCCGCACAAAATCGTACTG GCAGACGCCAAAATTGCCGATGCAGGCAAAATCCTTTCGCGTATGTGCTTCGAAGCCAAC GCTGACTGGGTGACGGTAATTTGCTGTGCGGATATCAACACCGCCAAAGGCGCGCTGGAC GTGGCAAAAGAGTTTAACGGCGACGTGCAGATCGAACTGACCGGTTACTGGACCTGGGAA CAGGCGCAACAGTGGCGCGATGCAGGCATTGGGCAGGTGGTTTATCACCGCAGCCGTGAC GCGCAGGCCGCAGGCGTGGCGTGGGGCGAAGCGGACATCACCGCGATCAAACGTCTTTCC GATATGGGCTTCAAAGTCACCGTCACCGGAGGCCTGGCGCTGGAAGATCTGCCGCTGTTC AAGGGTATTCCGATTCACGTCTTTATCGCGGGCCGTAGTATCCGTGATGCCGCTTCTCCG GTGGAAGCCGCACGTCAGTTCAAACGTTCCATCGCTGAACTGTGGGGCTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P39304 UniProtKB Entry Name ULAD_ECOLI GenBank Protein ID 537037 GenBank Gene ID U14003 - General References
- Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Reizer J, Reizer A, Saier MH Jr: Is the ribulose monophosphate pathway widely distributed in bacteria? Microbiology. 1997 Aug;143 ( Pt 8):2519-20. [Article]
- Yew WS, Gerlt JA: Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons. J Bacteriol. 2002 Jan;184(1):302-6. [Article]
- Campos E, Aguilar J, Baldoma L, Badia J: The gene yjfQ encodes the repressor of the yjfR-X regulon (ula), which is involved in L-ascorbate metabolism in Escherichia coli. J Bacteriol. 2002 Nov;184(21):6065-8. [Article]
- Campos E, Baldoma L, Aguilar J, Badia J: Regulation of expression of the divergent ulaG and ulaABCDEF operons involved in LaAscorbate dissimilation in Escherichia coli. J Bacteriol. 2004 Mar;186(6):1720-8. [Article]
- Yew WS, Wise EL, Rayment I, Gerlt JA: Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: mechanistic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry. 2004 Jun 1;43(21):6427-37. [Article]
- Yew WS, Akana J, Wise EL, Rayment I, Gerlt JA: Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: enhancing the promiscuous D-arabino-hex-3-ulose 6-phosphate synthase reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry. 2005 Feb 15;44(6):1807-15. [Article]
- Wise E, Yew WS, Babbitt PC, Gerlt JA, Rayment I: Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry. 2002 Mar 26;41(12):3861-9. [Article]
- Wise EL, Yew WS, Gerlt JA, Rayment I: Structural evidence for a 1,2-enediolate intermediate in the reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase, a member of the orotidine 5'-monophosphate decarboxylase suprafamily. Biochemistry. 2003 Oct 28;42(42):12133-42. [Article]
- Wise EL, Yew WS, Gerlt JA, Rayment I: Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: crystallographic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry. 2004 Jun 1;43(21):6438-46. [Article]
- Wise EL, Yew WS, Akana J, Gerlt JA, Rayment I: Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: structural basis for catalytic promiscuity in wild-type and designed mutants of 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry. 2005 Feb 15;44(6):1816-23. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01655 L-gulonic acid 6-phosphate experimental unknown Details DB01923 L-Xylulose 5-Phosphate experimental unknown Details DB02630 L-xylitol 5-phosphate experimental unknown Details DB03855 L-Threonohydroxamate 4-Phosphate experimental unknown Details DB04034 Ribulose-5-Phosphate experimental unknown Details