Quinate/shikimate dehydrogenase (P0A6D5)

Identification
Name:Quinate/shikimate dehydrogenase
Synonyms:
  • NAD-dependent shikimate 5-dehydrogenase 2
Gene Name:ydiB
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:The physiological substrate is not known
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
  • Metabolic pathways eco01100
  • Phenylalanine, tyrosine and tryptophan biosynthesis ec00400
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.03-Dehydro-shikimate + 1.0Hydrogen ion + 1.0NADPH ↔ 1.0NADP + 1.0Shikimic acid
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+2.0Thumb+1.0Thumb
1.0NAD + 1.0Quinate ↔ 1.03-Dehydroquinate + 2.0Hydrogen ion + 1.0NADH
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Quinate + 1.0NAD ↔ 1.03-Dehydroquinate + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Shikimic acid + 1.0NADP ↔ 1.03-Dehydro-shikimate + 1.0NADPH + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Quinate + 1.0NADP ↔ 1.03-Dehydroquinate + 1.0NADPH + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Shikimic acid + 1.0NAD ↔ 1.03-Dehydro-shikimate + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Quinate + 1.0NAD + 1.0NADP + 1.0Shikimic acid ↔ 1.03-Dehydroquinate + 1.0NADH + 1.0NADPH + 1.0Hydrogen ion + 1.03-Dehydro-shikimate
ReactionCard
SMPDB Reactions:
1.03-dehydroshikimate+1.0Thumb+1.0NADPH+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.03-dehydroshikimate + 1.0Hydrogen ion + 1.0NADPH + 1.03-Dehydro-shikimate + 1.0NADPH → 1.0NADP + 1.0Shikimic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.03-Dehydro-shikimate + 1.0Hydrogen ion + 1.0NADPH ↔ 1.0NADP + 1.0Shikimic acid
ReactionCard
Complex Reactions:
1.0Thumb+1.0NAD(P)(+) → 1.0Thumb+1.0NAD(P)H
1.0Quinate + 1.0NAD(P)(+) → 1.03-Dehydroquinate + 1.0NAD(P)H
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB040483-Dehydro-shikimateMetaboCard
ECMDB040493-DehydroquinateMetaboCard
ECMDB02260Gallic acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
ECMDB21278QuinateMetaboCard
ECMDB03070Shikimic acidMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
shikimate 5-dehydrogenase activity
Process
metabolic process
oxidation reduction
Gene Properties
Blattner:b1692
Gene OrientationClockwise
Centisome Percentage:38.19
Left Sequence End1771813
Right Sequence End1772679
Gene Sequence:
>867 bp
ATGAAGTATGTCTTTATTGAAAAACATCAGGCTGAGTTCAGCATCAAAGCAATGTGCCGC
GTGCTCCGGGTGGCCCGCAGCGGCTGGTATACGTGGTGTCAGCGGCGGACAAGGATAAGC
ACGCGTCAGCAGTTCCGCCAACACTGCGACAGCGTTGTCCTCGCGGCTTTTACCCGGTCA
AAACAGCGTTACGGTGCCCCACGCCTGACGGATGAACTGCGTGCTCAGGGTTACCCCTTT
AACGTAAAAACCGTGGCGGCAAGCCTGCGCCGTCAGGGACTGAGGGCAAAGGCCTCCCGG
AAGTTCAGCCCGGTCAGCTACCGCGCACACGGCCTGCCTGTGTCAGAAAATCTGTTGGAG
CAGGATTTTTACGCCAGTGGCCCGAACCAGAAGTGGGCAGGAGACATCACGTACTTACGT
ACAGATGAAGGCTGGCTGTATCTGGCAGTGGTCATTGACCTGTGGTCACGTGCCGTTATT
GGCTGGTCAATGTCGCCACGCATGACGGCGCAACTGGCCTGCGATGCCCTGCAGATGGCG
CTGTGGCGGCGTAAGAGGCCCCGGAACGTTATCGTTCACACGGACCGTGGAGGCCAGTAC
TGTTCAGCAGATTATCAGGCGCAACTGAAGCGGCATAATCTGCGTGGAAGTATGAGCGCA
AAAGGTTGCTGCTACGATAATGCCTGCGTGGAAAGCTTCTTTCATTCGCTGAAAGTGGAA
TGTATCCATGGAGAACACTTTATCAGCCGGGAAATAATGCGGGCAACGGTGTTTAATTAT
ATCGAATGTGATTACAATCGGTGGCGGCGGCACAGTTGGTGTGGCGGCCTCAGTCCGGAA
CAATTTGAAAACAAGAACCTCGCTTAG
Protein Properties
Pfam Domain Function:
Protein Residues:288
Protein Molecular Weight:31228
Protein Theoretical pI:5
PDB File:1VI2
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Quinate/shikimate dehydrogenase
MDVTAKYELIGLMAYPIRHSLSPEMQNKALEKAGLPFTYMAFEVDNDSFPGAIEGLKALK
MRGTGVSMPNKQLACEYVDELTPAAKLVGAINTIVNDDGYLRGYNTDGTGHIRAIKESGF
DIKGKTMVLLGAGGASTAIGAQGAIEGLKEIKLFNRRDEFFDKALAFAQRVNENTDCVVT
VTDLADQQAFAEALASADILTNGTKVGMKPLENESLVNDISLLHPGLLVTECVYNPHMTK
LLQQAQQAGCKTIDGYGMLLWQGAEQFTLWTGKDFPLEYVKQVMGFGA
References
External Links:
ResourceLink
Uniprot ID:P0A6D5
Uniprot Name:YDIB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674444
PDB ID:1VI2
Ecogene ID:EG11234
Ecocyc:EG11234
ColiBase:b1692
Kegg Gene:b1692
EchoBASE ID:EB1216
CCDB:YDIB_ECOLI
BacMap:16129648
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • Badger, J., Sauder, J. M., Adams, J. M., Antonysamy, S., Bain, K., Bergseid, M. G., Buchanan, S. G., Buchanan, M. D., Batiyenko, Y., Christopher, J. A., Emtage, S., Eroshkina, A., Feil, I., Furlong, E. B., Gajiwala, K. S., Gao, X., He, D., Hendle, J., Huber, A., Hoda, K., Kearins, P., Kissinger, C., Laubert, B., Lewis, H. A., Lin, J., Loomis, K., Lorimer, D., Louie, G., Maletic, M., Marsh, C. D., Miller, I., Molinari, J., Muller-Dieckmann, H. J., Newman, J. M., Noland, B. W., Pagarigan, B., Park, F., Peat, T. S., Post, K. W., Radojicic, S., Ramos, A., Romero, R., Rutter, M. E., Sanderson, W. E., Schwinn, K. D., Tresser, J., Winhoven, J., Wright, T. A., Wu, L., Xu, J., Harris, T. J. (2005). "Structural analysis of a set of proteins resulting from a bacterial genomics project." Proteins 60:787-796. Pubmed: 16021622
  • Benach, J., Lee, I., Edstrom, W., Kuzin, A. P., Chiang, Y., Acton, T. B., Montelione, G. T., Hunt, J. F. (2003). "The 2.3-A crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase." J Biol Chem 278:19176-19182. Pubmed: 12624088
  • 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
  • Duncan, K., Chaudhuri, S., Campbell, M. S., Coggins, J. R. (1986). "The overexpression and complete amino acid sequence of Escherichia coli 3-dehydroquinase." Biochem J 238:475-483. Pubmed: 3541912
  • 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
  • Johansson, L., Liden, G. (2006). "Transcriptome analysis of a shikimic acid producing strain of Escherichia coli W3110 grown under carbon- and phosphate-limited conditions." J Biotechnol 126:528-545. Pubmed: 16828913
  • Lindner, H. A., Nadeau, G., Matte, A., Michel, G., Menard, R., Cygler, M. (2005). "Site-directed mutagenesis of the active site region in the quinate/shikimate 5-dehydrogenase YdiB of Escherichia coli." J Biol Chem 280:7162-7169. Pubmed: 15596430
  • Michel, G., Roszak, A. W., Sauve, V., Maclean, J., Matte, A., Coggins, J. R., Cygler, M., Lapthorn, A. J. (2003). "Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities." J Biol Chem 278:19463-19472. Pubmed: 12637497