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InterPro: IPR016037 3-dehydroquinate synthase AroB, subgroup

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UniProtKB

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1644 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
Matches in BioMart

Accession

IPR016037 DHQ_synth_AroB_sub

Type

Domain

Signatures Help

Database	ID	Name	Proteins
HAMAP	MF_00110	AROB_MF_00110	1393
TIGRFAMs	TIGR01357	aroB	1585
Signatures in BioMart

InterPro Relationships Help

Parent

IPR002658 3-dehydroquinate synthase AroB

Found in

IPR008289 Pentafunctional AroM protein
IPR016303 3-dehydroquinate synthase

GO Term annotation Help

Process

GO:0009073 aromatic amino acid family biosynthetic process

Function

GO:0003856 3-dehydroquinate synthase activity

Component

GO:0005737 cytoplasm

InterPro annotation

Entry Details in BioMart

Abstract

The 3-dehydroquinate synthase (EC:4.2.3.4) 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 links Help

PDB - click here

SCOP: e.22.1.1

CATH: 1.20.1090.10 , 3.40.50.1970

Database links Help

Enzyme: EC:4.2.3.4

CluSTr: ALLvsALL:31178:69.2

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR016037

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A1RVE1 3-dehydroquinate synthase

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
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

Publications Open in usermanual
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 Reading Open in usermanual
	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
	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

InterPro 23.1