L-xylulose/3-keto-L-gulonate kinase (P37677)

Identification
Name:L-xylulose/3-keto-L-gulonate kinase
Synonyms:
  • L-xylulokinase
  • 3-dehydro-L-gulonate kinase
Gene Name:lyx
Enzyme Class:
Biological Properties
General Function:Involved in phosphotransferase activity, alcohol group as acceptor
Specific Function:Catalyzes the phosphorylation of L-xylulose and 3-keto- L-gulonate. Is involved in L-lyxose utilization via xylulose, and may also be involved in the utilization of 2,3-diketo-L-gulonate
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
  • Ascorbate and aldarate metabolism ec00053
  • Pentose and glucuronate interconversions ec00040
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0L-Threo-2-pentulose ↔ 1.0ADP + 1.0Hydrogen ion + 1.0L-Xylulose 5-phosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.03-Dehydro-L-gulonate + 1.0Adenosine triphosphate → 1.03-Dehydro-L-gulonate 6-phosphate + 1.0ADP + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0L-Threo-2-pentulose ↔ 1.0ADP + 1.0L-Xylulose 5-phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.03-Dehydro-L-gulonate + 1.0Adenosine triphosphate ↔ 1.03-Dehydro-L-gulonate 6-phosphate + 1.0ADP
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.03-keto-L-gulonate 6-phosphate+1.0Adenosine diphosphate+1.0Thumb+1.0Thumb+1.0Thumb
1.03-Dehydro-L-gulonate + 1.0Adenosine triphosphate → 1.03-keto-L-gulonate 6-phosphate + 1.0Adenosine diphosphate + 1.0Hydrogen ion + 1.03-Keto-L-gulonate 6-phosphate + 1.0ADP
ReactionCard
1.0L-Threo-2-pentulose+1.0Thumb+1.0Thumb → 1.0Xylulose 5-phosphate+1.0Adenosine diphosphate+1.0Thumb+1.0Thumb
1.0L-Threo-2-pentulose + 1.0Adenosine triphosphate + 1.0L-Threo-2-pentulose → 1.0Xylulose 5-phosphate + 1.0Adenosine diphosphate + 1.0Xylulose 5-phosphate + 1.0ADP
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Threo-2-pentulose + 1.0Adenosine triphosphate → 1.0L-Xylulose 5-phosphate + 1.0ADP + 1.0Hydrogen ion
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.03-Dehydro-L-gulonate + 1.0Adenosine triphosphate → 1.03-Dehydro-L-gulonate 6-phosphate + 1.0ADP + 1.0Hydrogen ion
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0L-Threo-2-pentulose → 1.0ADP + 1.0L-Xylulose 5-phosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.03-Dehydro-L-gulonate → 1.0ADP + 1.03-Dehydro-L-gulonate 6-phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB063343-Dehydro-L-gulonateMetaboCard
ECMDB200673-Dehydro-L-gulonate 6-phosphateMetaboCard
ECMDB202713-Keto-L-gulonate 6-phosphateMetaboCard
ECMDB214943-Keto-L-gulonic acidMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00751L-Threo-2-pentuloseMetaboCard
ECMDB20169L-Xylulose 5-phosphateMetaboCard
ECMDB04178Xylulose 5-phosphateMetaboCard
GO Classification:
Function
catalytic activity
phosphotransferase activity, alcohol group as acceptor
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
carbohydrate metabolic process
metabolic process
primary metabolic process
Gene Properties
Blattner:b3580
Gene OrientationClockwise
Centisome Percentage:80.72
Left Sequence End3745107
Right Sequence End3746603
Gene Sequence:
>1497 bp
ATGGCTCACCCTCATTTATTAGCGGAAAGAATTTCCCGCCTGAGCAGTTCGTTGGAAAAG
GGGCTTTATGAACGTAGCCACGCCATCCGCTTGTGTTTATTAGCGGCATTAAGTGGTGAA
AGTGTGTTCCTCCTTGGCCCGCCAGGTATTGCCAAAAGTTTGATCGCCCGGCGCTTAAAA
TTCGCCTTTCAGAATGCCCGCGCGTTTGAATATCTGATGACCCGCTTCTCCACGCCGGAA
GAAGTTTTTGGTCCCCTTTCTATTCAGGCGCTAAAAGATGAAGGGCGCTATGAACGTTTA
ACCAGCGGTTACCTGCCGGAAGCAGAAATTGTCTTTCTGGATGAGATCTGGAAAGCGGGC
CCGGCAATTCTTAATACCTTGCTCACCGCCATTAACGAGCGCCAGTTCCGCAACGGTGCA
CACGTAGAAAAAATCCCGATGCGTCTGCTGGTGGCGGCCTCCAACGAGCTGCCGGAAGCA
GACAGCAGTCTGGAAGCGTTATATGACCGCATGCTGATTCGTCTGTGGTTAGATAAAGTG
CAGGATAAAGCGAATTTCCGCTCCATGCTGACCAGTCAACAGGATGAAAACGACAATCCG
GTTCCTGATGCCTTGCAGGTCACAGATGAAGAATATGAACGCTGGCAGAAAGAGATTGGT
GAAATTACGCTGCCCGATCATGTATTTGAGCTGATTTTTATGCTGCGCCAGCAACTGGAT
AAATTACCGGATGCGCCTTATGTCTCGGATCGTCGCTGGAAAAAAGCGATCCGATTATTG
CAGGCCAGCGCCTTTTTTAGCGGTCGCAGTGCTGTTGCCCCGGTAGATCTCATTTTGCTG
AAAGATTGCCTGTGGTATGACGCGCAAAGCCTGAATTTGATACAACAACAAATTGATGTA
TTGATGACCGGTCACGCCTGGCAACAGCAAGGGATGTTGACTCGCCTTGGCGCGATTGTG
CAACGTCACCTGCAACTCCAGCAGCAACAAAGCGATAAAACAGCCTTAACGGTAATTCGT
CTGGGCGGCATTTTCAGCCGTCGTCAGCAGTATCAACTTCCTGTTAACGTTACTGCTTCC
ACTCTGACTCTACTGCTGCAAAAACCGTTAAAACTGCATGATATGGAAGTGGTTCATATC
TCCTTTGAGCGTAGCGCGCTGGAACAGTGGCTGAGCAAAGGTGGTGAAATTCGCGGTAAA
CTGAACGGTATCGGCTTTGCCCAGAAACTGAATCTGGAAGTTGATAGCGCCCAACATCTT
GTCGTTCGCGATGTAAGTTTACAAGGCAGTACGCTGGCACTTCCCGGTTCATCGGCTGAA
GGTCTGCCTGGTGAAATAAAACAACAACTGGAAGAGCTTGAAAGCGACTGGCGCAAGCAA
CACGCTTTATTCAGCGAACAGCAAAAATGTCTGTTTATCCCTGGCGACTGGTTAGGTCGC
ATTGAAGCCAGCCTACAGGATGTCGGTGCACAGATTCGCCAGGCACAACAATGCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:498
Protein Molecular Weight:55155
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>L-xylulose/3-keto-L-gulonate kinase
MTQYWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIR
ALLTHSGVSGEQIVGIGISAQGKGLFLLDKNDKPLGNAILSSDRRAMEIVRRWQEDGIPE
KLYPLTRQTLWTGHPVSLLRWLKEHEPERYAQIGCVMMTHDYLRWCLTGVKGCEESNISE
SNLYNMSLGEYDPCLTDWLGIAEINHALPPVVGSAEICGEITAQTAALTGLKAGTPVVGG
LFDVVSTALCAGIEDEFTLNAVMGTWAVTSGITRGLRDGEAHPYVYGRYVNDGEFIVHEA
SPTSSGNLEWFTAQWGEISFDEINQAVASLPKAGGDLFFLPFLYGSNAGLEMTSGFYGMQ
AIHTRAHLLQAIYEGVVFSHMTHLNRMRERFTDVHTLRVTGGPAHSDVWMQMLADVSGLR
IELPQVEETGCFGAALAARVGTGVYHNFSEAQRDLRHPVRTLLPDMTAHQLYQKKYQRYQ
HLIAALQGFHARIKEHTL
References
External Links:
ResourceLink
Uniprot ID:P37677
Uniprot Name:LYXK_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85676292
Ecogene ID:EG12284
Ecocyc:EG12284
ColiBase:b3580
Kegg Gene:b3580
EchoBASE ID:EB2192
CCDB:LYXK_ECOLI
BacMap:16131451
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
  • 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
  • Sanchez, J. C., Gimenez, R., Schneider, A., Fessner, W. D., Baldoma, L., Aguilar, J., Badia, J. (1994). "Activation of a cryptic gene encoding a kinase for L-xylulose opens a new pathway for the utilization of L-lyxose by Escherichia coli." J Biol Chem 269:29665-29669. Pubmed: 7961955
  • Sofia, H. J., Burland, V., Daniels, D. L., Plunkett, G. 3rd, Blattner, F. R. (1994). "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Nucleic Acids Res 22:2576-2586. Pubmed: 8041620
  • 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