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InterPro: IPR002658 3-dehydroquinate synthase AroB

Protein matchesHelp
UniProtKB
Matches:
2112 proteins
AccessionHelp IPR002658 DHQ_synth_AroB
SecondaryHelp IPR006265
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR016037 3-dehydroquinate synthase AroB, subgroup
GO Term annotationHelp
Process GO:0009073 aromatic amino acid family biosynthetic process
Function GO:0003856 3-dehydroquinate synthase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

The 3-dehydroquinate synthase (EC:4.6.1.3) domain is present in isolation in various bacterial 3-dehydroquinate synthases and also present as a domain in the pentafunctional AROM polypeptide (P07547) [1]. 3-dehydroquinate (DHQ) synthase catalyses the formation of dehydroquinate (DHQ) and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate [2]. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.

Structural linksHelp
SCOP: e.22.1.1
Database linksHelp
Enzyme: EC:4.2.3.4
PANDIT: PF01761
Blocks: IPB002658
Pfam Clan: CL0224.4

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR002658 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
A0B5P3 Glycerol-1-phosphate dehydrogenase [NAD(P)+]

P07547 Pentafunctional AROM polypeptide

P08566 Pentafunctional AROM polypeptide

P56081 3-dehydroquinate synthase

P73997 3-dehydroquinate synthase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR013785 Aldolase-type TIM barrel
IPR016303 3-dehydroquinate synthase
IPR013792 RNA 3'-terminal phosphate cyclase/enolpyruvate transferase, alpha/beta
IPR002658 3-dehydroquinate synthase AroB
IPR013708 Shikimate dehydrogenase substrate binding, N-terminal
IPR010110 Shikimate-5-dehydrogenase
IPR008289 Pentafunctional AroM protein
IPR016037 3-dehydroquinate synthase AroB, subgroup
IPR018508 3-dehydroquinate dehydratase, active site
IPR001381 Dehydroquinase class I
IPR000623 Shikimate kinase
IPR016040 NAD(P)-binding domain
IPR016205 Glycerol dehydrogenase
IPR006151 Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
IPR006264 3-phosphoshikimate 1-carboxyvinyltransferase, subgroup
IPR001986 3-phosphoshikimate 1-carboxyvinyltransferase, core
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Hawkins AR, Lamb HK.
The molecular biology of multidomain proteins. Selected examples.
Eur. J. Biochem. 232 7-18 1995 [PubMed: 7556173]
http://dx.doi.org/10.1111/j.1432-1033.1995.tb20775.x
2. Barten R, Meyer TF.
Cloning and characterisation of the Neisseria gonorrhoeae aroB gene.
Mol. Gen. Genet. 258 34-44 1998 [PubMed: 9613570]
http://dx.doi.org/10.1007/s004380050704

Additional ReadingHelp
Carpenter EP, Hawkins AR, Frost JW, Brown KA.
Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis.
Nature 394 1998 299-302 [PubMed: 9685163]
http://dx.doi.org/10.1038/28431
Nichols CE, Ren J, Lamb HK, Hawkins AR, Stammers DK.
Ligand-induced conformational changes and a mechanism for domain closure in Aspergillus nidulans dehydroquinate synthase.
J. Mol. Biol. 327 2003 129-44 [PubMed: 12614613]
http://dx.doi.org/10.1016/S0022-2836(03)00086-X
Sugahara M, Nodake Y, Sugahara M, Kunishima N.
Crystal structure of dehydroquinate synthase from Thermus thermophilus HB8 showing functional importance of the dimeric state.
Proteins 58 2005 249-52 [PubMed: 15508124]
http://dx.doi.org/10.1002/prot.20281
Nichols CE, Hawkins AR, Stammers DK.
Structure of the 'open' form of Aspergillus nidulans 3-dehydroquinate synthase at 1.7 A resolution from crystals grown following enzyme turnover.
Acta Crystallogr. D Biol. Crystallogr. 60 2004 971-3 [PubMed: 15103156]
http://dx.doi.org/10.1107/S0907444904004743
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InterPro 23.1