L-ribulose-5-phosphate 3-epimerase ulaE (P39305)

Identification
Name:L-ribulose-5-phosphate 3-epimerase ulaE
Synonyms:
  • L-ascorbate utilization protein E
  • L-xylulose-5-phosphate 3-epimerase
Gene Name:ulaE
Enzyme Class:
Biological Properties
General Function:Involved in intramolecular oxidoreductase activity, interconverting aldoses and ketoses
Specific Function:Catalyzes the isomerization of L-xylulose-5-phosphate to L-ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate utilization
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb
1.0L-Xylulose 5-phosphate ↔ 1.0L-Ribulose 5-phosphate
ReactionCard
1.0Thumb ↔ 1.0Thumb
1.0L-Ribulose 5-phosphate ↔ 1.0L-Xylulose 5-phosphate
ReactionCard
SMPDB Reactions:
1.0Xylulose 5-phosphate+1.0Thumb → 1.0 L-ribulose 5-phosphate+1.0Thumb
1.0Xylulose 5-phosphate + 1.0Xylulose 5-phosphate → 1.0 L-ribulose 5-phosphate + 1.0 L-ribulose 5-phosphate
ReactionCard
1.0L-xylulose -5-phosphate+1.0Thumb → 1.0 L-ribulose 5-phosphate+1.0Thumb
1.0L-xylulose -5-phosphate + 1.0L-Xylulose 5-phosphate → 1.0 L-ribulose 5-phosphate + 1.0 L-ribulose 5-phosphate
ReactionCard
1.0Thumb → 1.0Thumb
1.0L-Xylulose 5-phosphate → 1.0 L-ribulose 5-phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb ↔ 1.0Thumb
1.0L-Xylulose 5-phosphate ↔ 1.0L-Ribulose 5-phosphate
ReactionCard
1.0Thumb ↔ 1.0Thumb
1.0L-Ribulose 5-phosphate ↔ 1.0L-Xylulose 5-phosphate
ReactionCard
1.0Thumb ← 1.0Thumb
1.0L-Ribulose 5-phosphate ← 1.0L-Xylulose 5-phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB24194 L-ribulose 5-phosphateMetaboCard
ECMDB20167L-Ribulose 5-phosphateMetaboCard
ECMDB20169L-Xylulose 5-phosphateMetaboCard
ECMDB04178Xylulose 5-phosphateMetaboCard
GO Classification:
Function
catalytic activity
intramolecular oxidoreductase activity
intramolecular oxidoreductase activity, interconverting aldoses and ketoses
isomerase activity
Process
carbohydrate metabolic process
metabolic process
primary metabolic process
Gene Properties
Blattner:b4197
Gene OrientationClockwise
Centisome Percentage:95.28
Left Sequence End4420869
Right Sequence End4421723
Gene Sequence:
>855 bp
ATGACGCTATTTACAACCTTACTGGTGTTAATTTTCGAGCGCCTGTTTAAGTTGGGCGAG
CACTGGCAGCTTGATCATCGTCTTGAAGCGTTCTTTCGGCGGGTGAAACATTTTTCTCTC
GGGCGCACGTTAGGCATGACCATTATTGCGATGGGCGTGACTTTTTTACTGTTACGCGCA
TTGCAGGGAGTATTGTTCAACGTTCCCACGCTACTGGTGTGGCTGCTGATTGGTTTGCTG
TGTATTGGCGCAGGTAAAGTTCGTCTTCATTATCATGCTTATCTGACAGCTGCTTCACGT
AATGATAGCCATGCCCGTGCCACGATGGCTGGCGAACTCACCATGATTCACGGCGTCCCG
GCAGGCTGCGACGAACGTGAGTATTTGCGTGAGCTGCAAAATGCATTGCTGTGGATTAAC
TTTCGTTTTTATCTTGCACCGCTGTTCTGGCTGATTGTGGGGGGAACCTGGGGACCCGTT
ACGCTGATGGGGTATGCGTTTTTGCGTGCATGGCAATACTGGCTGGCGCGATATCAGACG
CCGCATCATCGTTTACAGTCCGGCATTGATGCCGTGCTTCATGTACTGGATTGGGTGCCG
GTTCGTCTTGCGGGTGTGGTATATGCCTTGATCGGTCATGGTGAGAAAGCGTTACCGGCC
TGGTTTGCTTCGCTGGGTGATTTCCATACTTCGCAGTATCAGGTGTTAACGCGTCTGGCG
CAGTTCTCTCTGGCGCGTGAACCGCATGTCGATAAGGTGGAGACGCCGAAGGCAGCGGTT
TCAATGGCGAAGAAAACCTCGTTCGTGGTCGTGGTGGTGATTGCACTACTGACGATTTAC
GGGGCGTTGGTGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:284
Protein Molecular Weight:32006
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>L-ribulose-5-phosphate 3-epimerase ulaE
MLSKQIPLGIYEKALPAGECWLERLQLAKTLGFDFVEMSVDETDDRLSRLNWSREQRLAL
VNAIVETGVRVPSMCLSAHRRFPLGSEDDAVRAQGLEIMRKAIQFAQDVGIRVIQLAGYD
VYYQEANNETRRRFRDGLKESVEMASRAQVTLAMEIMDYPLMSSISKALGYAHYLNNPWF
QLYPDIGNLSAWDNDVQMELQAGIGHIVAVHVKDTKPGVFKNVPFGEGVVDFERCFETLK
QSGYCGPYLIEMWSETAEDPAAEVAKARDWVKARMAKAGMVEAA
References
External Links:
ResourceLink
Uniprot ID:P39305
Uniprot Name:ULAE_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21238959
Ecogene ID:EG12497
Ecocyc:EG12497
ColiBase:b4197
Kegg Gene:b4197
EchoBASE ID:EB2390
CCDB:ULAE_ECOLI
BacMap:16132019
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
  • 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