Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive
Details
- Name
- Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive
- Synonyms
- 2.5.1.54
- 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
- DAHP synthase
- Phospho-2-keto-3-deoxyheptonate aldolase
- Gene Name
- aroG
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0011443|Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive MNYQNDDLRIKEIKELLPPVALLEKFPATENAANTVAHARKAIHKILKGNDDRLLVVIGP CSIHDPVAAKEYATRLLALREELKDELEIVMRVYFEKPRTTVGWKGLINDPHMDNSFQIN DGLRIARKLLLDINDSGLPAAGEFLDMITPQYLADLMSWGAIGARTTESQVHRELASGLS CPVGFKNGTDGTIKVAIDAINAAGAPHCFLSVTKWGHSAIVNTSGNGDCHIILRGGKEPN YSAKHVAEVKEGLNKAGLPAQVMIDFSHANSSKQFKKQMDVCADVCQQIAGGEKAIIGVM VESHLVEGNQSLESGEPLAYGKSITDACIGWEDTDALLRQLANAVKARRG
- Number of residues
- 350
- Molecular Weight
- 38009.165
- Theoretical pI
- 6.58
- GO Classification
- Functions3-deoxy-7-phosphoheptulonate synthase activity / identical protein bindingProcessesaromatic amino acid family biosynthetic process / chorismate biosynthetic processComponentscytosol
- General Function
- Identical protein binding
- Specific Function
- Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
- Pfam Domain Function
- DAHP_synth_1 (PF00793)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011444|Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive (aroG) ATGAATTATCAGAACGACGATTTACGCATCAAAGAAATCAAAGAGTTACTTCCTCCTGTC GCATTGCTGGAAAAATTCCCCGCTACTGAAAATGCCGCGAATACGGTTGCCCATGCCCGA AAAGCGATCCATAAGATCCTGAAAGGTAATGATGATCGCCTGTTGGTTGTGATTGGCCCA TGCTCAATTCATGATCCTGTCGCGGCAAAAGAGTATGCCACTCGCTTGCTGGCGCTGCGT GAAGAGCTGAAAGATGAGCTGGAAATCGTAATGCGCGTCTATTTTGAAAAGCCGCGTACC ACGGTGGGCTGGAAAGGGCTGATTAACGATCCGCATATGGATAATAGCTTCCAGATCAAC GACGGTCTGCGTATAGCCCGTAAATTGCTGCTTGATATTAACGACAGCGGTCTGCCAGCG GCAGGTGAGTTTCTCGATATGATCACCCCACAATATCTCGCTGACCTGATGAGCTGGGGC GCAATTGGCGCACGTACCACCGAATCGCAGGTGCACCGCGAACTGGCATCAGGGCTTTCT TGTCCGGTCGGCTTCAAAAATGGCACCGACGGTACGATTAAAGTGGCTATCGATGCCATT AATGCCGCCGGTGCGCCGCACTGCTTCCTGTCCGTAACGAAATGGGGGCATTCGGCGATT GTGAATACCAGCGGTAACGGCGATTGCCATATCATTCTGCGCGGCGGTAAAGAGCCTAAC TACAGCGCGAAGCACGTTGCTGAAGTGAAAGAAGGGCTGAACAAAGCAGGCCTGCCAGCA CAGGTGATGATCGATTTCAGCCATGCTAACTCGTCCAAACAATTCAAAAAGCAGATGGAT GTTTGTGCTGACGTTTGCCAGCAGATTGCCGGTGGCGAAAAGGCCATTATTGGCGTGATG GTGGAAAGCCATCTGGTGGAAGGCAATCAGAGCCTCGAGAGCGGGGAGCCGCTGGCCTAC GGTAAGAGCATCACCGATGCCTGCATCGGCTGGGAAGATACCGATGCTCTGTTACGTCAA CTGGCGAATGCAGTAAAAGCGCGTCGCGGGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0AB91 UniProtKB Entry Name AROG_ECOLI GenBank Protein ID 145368 GenBank Gene ID J01591 - General References
- Davies WD, Davidson BE: The nucleotide sequence of aroG, the gene for 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (phe) in Escherichia coli K12. Nucleic Acids Res. 1982 Jul 10;10(13):4045-58. [Article]
- Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [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]
- Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
- Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y: Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics. 2009 Feb;8(2):215-25. doi: 10.1074/mcp.M800187-MCP200. Epub 2008 Aug 23. [Article]
- Shumilin IA, Kretsinger RH, Bauerle RH: Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli. Structure. 1999 Jul 15;7(7):865-75. [Article]