3-keto-L-gulonate-6-phosphate decarboxylase ulaD (P39304)

Identification
Name:3-keto-L-gulonate-6-phosphate decarboxylase ulaD
Synonyms:
  • 3-dehydro-L-gulonate-6-phosphate decarboxylase
  • KGPDC
  • L-ascorbate utilization protein D
Gene Name:ulaD
Enzyme Class:
Biological Properties
General Function:Involved in magnesium ion binding
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
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
  • Ascorbate and aldarate metabolism ec00053
  • Metabolic pathways eco01100
  • Microbial metabolism in diverse environments ec01120
  • Pentose and glucuronate interconversions ec00040
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.03-Dehydro-L-gulonate 6-phosphate + 1.0Hydrogen ion ↔ 1.0Carbon dioxide + 1.0L-Xylulose 5-phosphate
ReactionCard
SMPDB Reactions:
1.03-keto-L-gulonate 6-phosphate+1.0Thumb+1.0Thumb → 1.0Xylulose 5-phosphate+1.0Thumb+1.0Thumb
1.03-keto-L-gulonate 6-phosphate + 1.0Hydrogen ion + 1.03-Keto-L-gulonate 6-phosphate → 1.0Xylulose 5-phosphate + 1.0Carbon dioxide + 1.0Xylulose 5-phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.03-Dehydro-L-gulonate 6-phosphate + 1.0Hydrogen ion ↔ 1.0Carbon dioxide + 1.0L-Xylulose 5-phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB200673-Dehydro-L-gulonate 6-phosphateMetaboCard
ECMDB202713-Keto-L-gulonate 6-phosphateMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB20169L-Xylulose 5-phosphateMetaboCard
ECMDB04178Xylulose 5-phosphateMetaboCard
GO Classification:
Function
carbon-carbon lyase activity
carboxy-lyase activity
catalytic activity
lyase activity
orotidine-5'-phosphate decarboxylase activity
Process
'de novo' pyrimidine base biosynthetic process
cellular aromatic compound metabolic process
cellular metabolic process
metabolic process
nucleobase metabolic process
pyrimidine base biosynthetic process
pyrimidine base metabolic process
Gene Properties
Blattner:b4196
Gene OrientationClockwise
Centisome Percentage:95.27
Left Sequence End4420209
Right Sequence End4420859
Gene Sequence:
>651 bp
ATGAAAGTATCAGTTCCAGGCATGCCGGTTACACTTTTAAATATGAGCAAGAACGATATT
TATAAGATGGTGAGCGGGGACAAGATGGACGTGAAGATGAATATCTTTCAACGCTTGTGG
GAGACGTTACGCCATCTGTTCTGGTCAGATAAACAGACTGAGGCTTATAAACTTCTGTTC
AATTTCGTGAATAACCAGACTGGCAACATCAACGCCTCAGAATACTTTACTGGGGCTATC
AACGAGAATGAGAGAGAAAAGTTTATCAATAGCCTGGAATTATTCAATAAACTTAAAACA
TGCGCAAAAAATCCGGATGAGTTGGTCGCAAAGGGCAATATGCGCTGGGTCGCCCAGACC
TTCGGGGATATCGAGTTAAGTGTCACTTTTTTCATTGAAAAGAATAAGATATGTACTCAG
ACGTTGCAGCTGCATAAGGGCCAAGGTAACTTGGGCGTTGATCTTAGAAAGGCTTACCTT
CCCGGCGTTGACATGAGGGATTGTTACCTTGGTAAAAAAACAATGAAAGGTAGCAATGAT
ATCCTTTATGAGAGACCTGGGTGGAATGCTAACCTGGGCGTGCTACCCCGGACGGTGCTA
CCCCGGACGGTGCTAACCCGGACGGTGCTAACCTGGACGGTGCTACCGTGA
Protein Properties
Pfam Domain Function:
Protein Residues:216
Protein Molecular Weight:23578
Protein Theoretical pI:5
PDB File:1XBV
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>3-keto-L-gulonate-6-phosphate decarboxylase ulaD
MSLPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALYPHKIVL
ADAKIADAGKILSRMCFEANADWVTVICCADINTAKGALDVAKEFNGDVQIELTGYWTWE
QAQQWRDAGIGQVVYHRSRDAQAAGVAWGEADITAIKRLSDMGFKVTVTGGLALEDLPLF
KGIPIHVFIAGRSIRDAASPVEAARQFKRSIAELWG
References
External Links:
ResourceLink
Uniprot ID:P39304
Uniprot Name:ULAD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674305
PDB ID:1XBV
Ecogene ID:EG12496
Ecocyc:EG12496
ColiBase:b4196
Kegg Gene:b4196
EchoBASE ID:EB2389
CCDB:ULAD_ECOLI
BacMap:16132018
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • Campos, E., Aguilar, J., Baldoma, L., Badia, J. (2002). "The gene yjfQ encodes the repressor of the yjfR-X regulon (ula), which is involved in L-ascorbate metabolism in Escherichia coli." J Bacteriol 184:6065-6068. Pubmed: 12374842
  • Campos, E., Baldoma, L., Aguilar, J., Badia, J. (2004). "Regulation of expression of the divergent ulaG and ulaABCDEF operons involved in LaAscorbate dissimilation in Escherichia coli." J Bacteriol 186:1720-1728. Pubmed: 14996803
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Reizer, J., Reizer, A., Saier, M. H. Jr (1997). "Is the ribulose monophosphate pathway widely distributed in bacteria?" Microbiology 143 ( Pt 8):2519-2520. Pubmed: 9274005
  • Wise, E. L., Yew, W. S., Akana, J., Gerlt, J. A., Rayment, I. (2005). "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 44:1816-1823. Pubmed: 15697207
  • Wise, E. L., Yew, W. S., Gerlt, J. A., Rayment, I. (2003). "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 42:12133-12142. Pubmed: 14567674
  • Wise, E. L., Yew, W. S., Gerlt, J. A., Rayment, I. (2004). "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 43:6438-6446. Pubmed: 15157078
  • Wise, E., Yew, W. S., Babbitt, P. C., Gerlt, J. A., Rayment, I. (2002). "Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase." Biochemistry 41:3861-3869. Pubmed: 11900527
  • Yew, W. S., Akana, J., Wise, E. L., Rayment, I., Gerlt, J. A. (2005). "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 44:1807-1815. Pubmed: 15697206
  • Yew, W. S., Gerlt, J. A. (2002). "Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons." J Bacteriol 184:302-306. Pubmed: 11741871
  • Yew, W. S., Wise, E. L., Rayment, I., Gerlt, J. A. (2004). "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 43:6427-6437. Pubmed: 15157077