D-erythro-7,8-dihydroneopterin triphosphate epimerase (P0AC19)

Identification
Name:D-erythro-7,8-dihydroneopterin triphosphate epimerase
Synonyms:
  • Dihydroneopterin triphosphate 2'-epimerase
Gene Name:folX
Enzyme Class:Not Available
Biological Properties
General Function:Involved in dihydroneopterin aldolase activity
Specific Function:Catalyzes the epimerization of carbon 2' of the side chain of dihydroneopterin triphosphate (H2NTP) to form dihydromonapterin triphosphate (H2MTP)
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:Not Available
SMPDB Reactions:
1.0Thumb ↔ 1.0Thumb
1.07,8-dihydroneopterin 3'-triphosphate ↔ 1.0Dihydromonapterin-triphosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb ↔ 1.0Thumb
1.0Dihydroneopterin triphosphate ↔ 1.0Dihydromonapterin-triphosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB242457,8-dihydroneopterin 3'-triphosphateMetaboCard
ECMDB20549Dihydromonapterin-triphosphateMetaboCard
ECMDB01144Dihydroneopterin triphosphateMetaboCard
GO Classification:
Function
aldehyde-lyase activity
carbon-carbon lyase activity
catalytic activity
dihydroneopterin aldolase activity
lyase activity
Process
cellular aromatic compound metabolic process
cellular metabolic process
folic acid and derivative metabolic process
metabolic process
Gene Properties
Blattner:b2303
Gene OrientationClockwise
Centisome Percentage:52.14
Left Sequence End2419347
Right Sequence End2419709
Gene Sequence:
>363 bp
ATGGATTACGAATTTCTGCGCGATATTACCGGAGTGGTAAAGGTGCGTATGTCCATGGGG
CATGAAGTGGTCGGGCACTGGTTTAATGAAGAGGTGAAAGAAAACCTGGCCTTGCTTGAT
GAAGTGGAACAAGCAGCGCACGCACTGAAAGGTAGCGAACGGTCCTGGCAACGGGCAGGG
CATGAATACACCCTGTGGATGGACGGTGAAGAGGTGATGGTTCGCGCCAATCAACTGGAA
TTCGCTGGCGATGAAATGGAAGAGGGGATGAACTACTACGACGAAGAAAGCCTGTCGCTA
TGCGGCGTTGAGGATTTTCTGCAGGTCGTGGCGGCTTACCGCAATTTCGTGCAGCAGAAG
TAA
Protein Properties
Pfam Domain Function:
Protein Residues:120
Protein Molecular Weight:14082
Protein Theoretical pI:7
PDB File:1B9L
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>D-erythro-7,8-dihydroneopterin triphosphate epimerase
MAQPAAIIRIKNLRLRTFIGIKEEEINNRQDIVINVTIHYPADKARTSEDINDALNYRTV
TKNIIQHVENNRFSLLEKLTQDVLDIAREHHWVTYAEVEIDKLHALRYADSVSMTLSWQR
References
External Links:
ResourceLink
Uniprot ID:P0AC19
Uniprot Name:FOLX_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21238972
PDB ID:1B9L
Ecogene ID:EG14263
Ecocyc:EG14263
ColiBase:b2303
Kegg Gene:b2303
EchoBASE ID:EB4011
CCDB:FOLX_ECOLI
BacMap:16130238
General Reference:
  • Ahn, C., Byun, J., Yim, J. (1997). "Purification, cloning, and functional expression of dihydroneopterin triphosphate 2'-epimerase from Escherichia coli." J Biol Chem 272:15323-15328. Pubmed: 9182560
  • 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
  • Haussmann, C., Rohdich, F., Lottspeich, F., Eberhardt, S., Scheuring, J., Mackamul, S., Bacher, A. (1997). "Dihydroneopterin triphosphate epimerase of Escherichia coli: purification, genetic cloning, and expression." J Bacteriol 179:949-951. Pubmed: 9006053
  • Haussmann, C., Rohdich, F., Schmidt, E., Bacher, A., Richter, G. (1998). "Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase." J Biol Chem 273:17418-17424. Pubmed: 9651328
  • 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
  • Ploom, T., Haussmann, C., Hof, P., Steinbacher, S., Bacher, A., Richardson, J., Huber, R. (1999). "Crystal structure of 7,8-dihydroneopterin triphosphate epimerase." Structure 7:509-516. Pubmed: 10378270
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837