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
Functions
3-deoxy-7-phosphoheptulonate synthase activity / identical protein binding
Processes
aromatic amino acid family biosynthetic process / chorismate biosynthetic process
Components
cytosol
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
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
ResourceLink
UniProtKB IDP0AB91
UniProtKB Entry NameAROG_ECOLI
GenBank Protein ID145368
GenBank Gene IDJ01591
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01819PhosphoenolpyruvateexperimentalunknownDetails
DB027262-Phosphoglycolic AcidexperimentalunknownDetails