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
Functions
3-dehydro-L-gulonate-6-phosphate decarboxylase activity / magnesium ion binding / orotidine-5'-phosphate decarboxylase activity
Processes
'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
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
ResourceLink
UniProtKB IDP39304
UniProtKB Entry NameULAD_ECOLI
GenBank Protein ID537037
GenBank Gene IDU14003
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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 IDNameDrug groupPharmacological action?ActionsDetails
DB01655L-gulonic acid 6-phosphateexperimentalunknownDetails
DB01923L-Xylulose 5-PhosphateexperimentalunknownDetails
DB02630L-xylitol 5-phosphateexperimentalunknownDetails
DB03855L-Threonohydroxamate 4-PhosphateexperimentalunknownDetails
DB04034Ribulose-5-PhosphateexperimentalunknownDetails