3-dehydroquinate synthase (P07639)

Identification
Name:3-dehydroquinate synthase
Synonyms:Not Available
Gene Name:aroB
Enzyme Class:
Biological Properties
General Function:Involved in 3-dehydroquinate synthase activity
Specific Function:3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
  • Metabolic pathways eco01100
  • Phenylalanine, tyrosine and tryptophan biosynthesis ec00400
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.02-Dehydro-3-deoxy-D-arabino-heptonate 7-phosphate ↔ 1.03-Dehydroquinate + 1.0Phosphate
ReactionCard
SMPDB Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.03-deoxy-D-arabino-heptulosonate-7-phosphate → 1.0Phosphate + 1.03-Dehydroquinate
ReactionCard
EcoCyc Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.02-Dehydro-3-deoxy-D-arabino-heptonate 7-phosphate ↔ 1.03-Dehydroquinate + 1.0Phosphate
ReactionCard
1.0Thumb → 1.0Thumb+1.0Thumb
1.02-Dehydro-3-deoxy-D-arabino-heptonate 7-phosphate → 1.0Phosphate + 1.03-Dehydroquinate
ReactionCard
Complex Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.02-Dehydro-3-deoxy-D-arabino-heptonate 7-phosphate → 1.03-Dehydroquinate + 1.0Inorganic phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB200392-Dehydro-3-deoxy-D-arabino-heptonate 7-phosphateMetaboCard
ECMDB040493-DehydroquinateMetaboCard
ECMDB241823-deoxy-D-arabino-heptulosonate-7-phosphateMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01429PhosphateMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
3-dehydroquinate synthase activity
carbon-oxygen lyase activity
carbon-oxygen lyase activity, acting on phosphates
catalytic activity
lyase activity
Process
aromatic amino acid family biosynthetic process
biosynthetic process
cellular amino acid and derivative metabolic process
cellular amino acid biosynthetic process
cellular amino acid metabolic process
cellular metabolic process
metabolic process
Gene Properties
Blattner:b3389
Gene OrientationCounterclockwise
Centisome Percentage:75.77
Left Sequence End3515420
Right Sequence End3516508
Gene Sequence:
>1089 bp
ATGAATTCATGTGATTTTCGTGTTTTTCTGCAAGAGTTCGGTACAACGGTTCATTTGTCA
TTGCCTGGTAGCGTATCCGAGAAAGAACGACTGCTACTCAAGCTGCTGATGCAGGGAATG
TCTGTAACAGAAATATCACAGTACAGAAATCGCAGTGCAAAGACAATTTCACATCAAAAG
AAACAGCTCTTTGAGAAACTGGGGATTCAGAGCGATATTACTTTCTGGCGCGATATTTTC
TTTCAGTACAATCCGGAGATCATATCCGCCACGGGGAGTAATAGTCACAGATATATTAAT
GATAATCACTATCACCATATCGTCACGCCTGAAGCCATCAGTCTGGCGTTGGAAAACCAC
GAATTCAAACCGTGGATCCAACCGGTTTTCTGCGCGCAGACTGGCGTACTGACGGGCTGT
GAGGTGCTTGTCCGCTGGGAACATCCACAAACGGGAATTATCCCACCGGATCAGTTTATT
CCTCTGGCGGAGTCATCCGGTCTTATTGTCATAATGACCCGCCAACTGATGAAACAGACT
GCGGATATTCTGATGCCGGTAAAACATTTGCTGCCGGACAATTTCCATATTGGCATCAAC
GTCTCGGCGGGTTGTTTTTTGGCAGCGGGATTTGAAAAAGAGTGTCTGAACCTGGTTAAT
AAATTAGGTAACGATAAAATCAAGCTGGTTCTCGAGCTAACGGAACGTAACCCTATTCCG
GTAACGCCAGAAGCCAGAGCGATATTTGACAGCCTTCATCAGCACAACATTACCTTTGCG
CTGGATGACTTTGGTACGGGTTATGCGACCTATCGTTACTTGCAGGCGTTCCCGGTCGAT
TTTATTAAGATCGATAAGTCATTTGTGCAAATGGCGAGTGTCGACGAAATCTCCGGTCAT
ATTGTGGACAATATTGTCGAACTAGCGCGTAAGCCTGGTCTGAGTATCGTGGCGGAAGGG
GTAGAAACCCAGGAGCAGGCGGATTTAATGATCGGTAAAGGCGTTCACTTTTTGCAGGGC
TATTTGTACTCTCCGCCAGTACCGGGTAATAAATTTATCTCTGAATGGGTAATGAAAGCA
GGTGGTTGA
Protein Properties
Pfam Domain Function:
Protein Residues:362
Protein Molecular Weight:38881
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>3-dehydroquinate synthase
MERIVVTLGERSYPITIASGLFNEPASFLPLKSGEQVMLVTNETLAPLYLDKVRGVLEQA
GVNVDSVILPDGEQYKSLAVLDTVFTALLQKPHGRDTTLVALGGGVVGDLTGFAAASYQR
GVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVVDLDCLKTLPPRELAS
GLAEVIKYGIILDGAFFNWLEENLDALLRLDGPAMAYCIRRCCELKAEVVAADERETGLR
ALLNLGHTFGHAIEAEMGYGNWLHGEAVAAGMVMAARTSERLGQFSSAETQRIITLLKRA
GLPVNGPREMSAQAYLPHMLRDKKVLAGEMRLILPLAIGKSEVRSGVSHELVLNAIADCQ
SA
References
External Links:
ResourceLink
Uniprot ID:P07639
Uniprot Name:AROB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674458
Ecogene ID:EG10074
Ecocyc:EG10074
ColiBase:b3389
Kegg Gene:b3389
EchoBASE ID:EB0072
CCDB:AROB_ECOLI
BacMap:16131267
General Reference:
  • Bender, S. L., Mehdi, S., Knowles, J. R. (1989). "Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis." Biochemistry 28:7555-7560. Pubmed: 2514789
  • 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
  • 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
  • Jonczyk, P., Hines, R., Smith, D. W. (1989). "The Escherichia coli dam gene is expressed as a distal gene of a new operon." Mol Gen Genet 217:85-96. Pubmed: 2549371
  • Lyngstadaas, A., Lobner-Olesen, A., Boye, E. (1995). "Characterization of three genes in the dam-containing operon of Escherichia coli." Mol Gen Genet 247:546-554. Pubmed: 7603433
  • Millar, G., Coggins, J. R. (1986). "The complete amino acid sequence of 3-dehydroquinate synthase of Escherichia coli K12." FEBS Lett 200:11-17. Pubmed: 3009224