Shikimate dehydrogenase (NADP(+))
Details
- Name
- Shikimate dehydrogenase (NADP(+))
- Synonyms
- 1.1.1.25
- SD
- Gene Name
- aroE
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0011385|Shikimate dehydrogenase (NADP(+)) METYAVFGNPIAHSKSPFIHQQFAQQLNIEHPYGRVLAPINDFINTLNAFFSAGGKGANV TVPFKEEAFARADELTERAALAGAVNTLMRLEDGRLLGDNTDGVGLLSDLERLSFIRPGL RILLIGAGGASRGVLLPLLSLDCAVTITNRTVSRAEELAKLFAHTGSIQALSMDELEGHE FDLIINATSSGISGDIPAIPSSLIHPGIYCYDMFYQKGKTPFLAWCEQRGSKRNADGLGM LVAQAAHAFLLWHGVLPDVEPVIKQLQEELSA
- Number of residues
- 272
- Molecular Weight
- 29413.305
- Theoretical pI
- 5.31
- GO Classification
- FunctionsNADP binding / nucleotide binding / shikimate 3-dehydrogenase (NADP+) activityProcessesaromatic amino acid family biosynthetic process / chorismate biosynthetic process / shikimate metabolic processComponentscytosol
- General Function
- Shikimate 3-dehydrogenase (nadp+) activity
- Specific Function
- Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). It displays no activity in the presence of NAD.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011386|Shikimate dehydrogenase (NADP(+)) (aroE) ATGGAAACCTATGCTGTTTTTGGTAATCCGATAGCCCACAGCAAATCGCCATTCATTCAT CAGCAATTTGCTCAGCAACTGAATATTGAACATCCCTATGGGCGCGTGTTGGCACCCATC AATGATTTCATCAACACACTGAACGCTTTCTTTAGTGCTGGTGGTAAAGGTGCGAATGTG ACGGTGCCTTTTAAAGAAGAGGCTTTTGCCAGAGCGGATGAGCTTACTGAACGGGCAGCG TTGGCTGGTGCTGTTAATACCCTCATGCGGTTAGAAGATGGACGCCTGCTGGGTGACAAT ACCGATGGTGTAGGCTTGTTAAGCGATCTGGAACGTCTGTCTTTTATCCGCCCTGGTTTA CGTATTCTGCTTATCGGCGCTGGTGGAGCATCTCGCGGCGTACTACTGCCACTCCTTTCC CTGGACTGTGCGGTGACAATAACTAATCGGACGGTATCCCGCGCGGAAGAGTTGGCTAAA TTGTTTGCGCACACTGGCAGTATTCAGGCGTTGAGTATGGACGAACTGGAAGGTCATGAG TTTGATCTCATTATTAATGCAACATCCAGTGGCATCAGTGGTGATATTCCGGCGATCCCG TCATCGCTCATTCATCCAGGCATTTATTGCTATGACATGTTCTATCAGAAAGGAAAAACT CCTTTTCTGGCATGGTGTGAGCAGCGAGGCTCAAAGCGTAATGCTGATGGTTTAGGAATG CTGGTGGCACAGGCGGCTCATGCCTTTCTTCTCTGGCACGGTGTTCTGCCTGACGTAGAA CCAGTTATAAAGCAATTGCAGGAGGAATTGTCCGCGTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P15770 UniProtKB Entry Name AROE_ECOLI GenBank Protein ID 40978 GenBank Gene ID Y00710 - General References
- Anton IA, Coggins JR: Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase. Biochem J. 1988 Jan 15;249(2):319-26. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Chaudhuri S, Coggins JR: The purification of shikimate dehydrogenase from Escherichia coli. Biochem J. 1985 Feb 15;226(1):217-23. [Article]
- Maclean J, Campbell SA, Pollock K, Chackrewarthy S, Coggins JR, Lapthorn AJ: Crystallization and preliminary X-ray analysis of shikimate dehydrogenase from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 2000 Apr;56(Pt 4):512-5. [Article]
- Michel G, Roszak AW, Sauve V, Maclean J, Matte A, Coggins JR, Cygler M, Lapthorn AJ: Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities. J Biol Chem. 2003 May 23;278(21):19463-72. Epub 2003 Mar 12. [Article]