Reviewed, UniProtKB/Swiss-Prot P43877 (AROQ_ACTPL)

Names and origin

Protein names

Recommended name:
    3-dehydroquinate dehydratase
      Short name=3-dehydroquinase
    EC=4.2.1.10
Alternative name(s):
    Type II DHQase

Gene names

Name:

aroQ

Organism

Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae)

Taxonomic identifier

715 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length	154 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes a trans-dehydration via an enolate intermediate By similarity.
Catalytic activity	3-dehydroquinate = 3-dehydroshikimate + H2O. HAMAP MF_00169
Pathway	Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. HAMAP MF_00169
Subunit structure	Homododecamer. Ref.2
Sequence similarities	Belongs to the type-II 3-dehydroquinase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Molecular function	Lyase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	3-dehydroquinate dehydratase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 154

154

3-dehydroquinate dehydratase HAMAP MF_00169

PRO_0000159862

Regions

Region

101 – 102

2

Substrate binding By similarity

Sites

Active site

23

1

Proton acceptor By similarity

Active site

100

1

Proton donor By similarity

Binding site

74

1

Substrate By similarity

Binding site

80

1

Substrate By similarity

Binding site

87

1

Substrate By similarity

Binding site

111

1

Substrate By similarity

Site

18

1

Transition state stabilizer By similarity

Secondary structure

1

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154

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Helix

12 – 14

3

Helix

20 – 22

3

Helix

28 – 41

14

Beta strand

45 – 50

6

Helix

54 – 63

10

Turn

64 – 67

4

Beta strand

70 – 74

5

Helix

78 – 81

4

Helix

83 – 92

10

Beta strand

96 – 102

7

Helix

104 – 106

3

Helix

109 – 111

3

Helix

117 – 119

3

Beta strand

120 – 127

8

Helix

130 – 144

15

Helix

147 – 151

5

Sequences

	Sequence		Length	Mass (Da)
	P43877-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 6DDC809E9B276BC4	FASTA	154	17,179
	10 20 30 40 50 60 MKKILLLNGP NLNMLGKREP HIYGSQTLSD IEQHLQQSAQ AQGYELDYFQ ANGEESLINR 70 80 90 100 110 120 IHQAFQNTDF IIINPGAFTH TSVAIRDALL AVSIPFIEVH LSNVHAREPF RHHSYLSDVA 130 140 150 KGVICGLGAK GYDYALDFAI SELQKIQLGE MMNG

References

[1]	"Characterization of a 3-dehydroquinase gene from Actinobacillus pleuropneumoniae with homology to the eukaryotic genes qa-2 and QUTE." Lalonde G., O'Hanley P.D., Stocker B.A.D., Denich K.T. Mol. Microbiol. 11:273-280(1994) [PubMed: 8170389] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S 4074 / Serotype 1.
[2]	"Structural study of the type II 3-dehydroquinate dehydratase from Actinobacillus pleuropneumoniae." Maes D., Gonzalez-Ramirez L.A., Lopez-Jaramillo J., Yu B., De Bondt H., Zegers I., Afonina E., Garcia-Ruiz J.M., Gulnik S. Acta Crystallogr. D 60:463-471(2004) [PubMed: 14993670] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L19895 Genomic DNA. Translation: AAA72027.1.

PIR

S41538.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UQR	X-ray	1.70	A/B/C/D/E/F/G/H/I/J/K/L	1-154	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

4.2.1.10. 257522.

Family and domain databases

HAMAP

MF_00169.
[Tree]

InterPro

IPR001874. DHquinase_II.
IPR018509. DHquinase_II_CS.
[Graphical view]

Gene3D

G3DSA:3.40.50.9100. DHquinase_II. 1 hit.

PANTHER

PTHR21272. DHquinase_II. 1 hit.

Pfam

PF01220. DHquinase_II. 1 hit.
[Graphical view]

PIRSF

PIRSF001399. DHquinase_II. 1 hit.

ProDom

PD004527. DHquinase_II. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01088. aroQ. 1 hit.

PROSITE

PS01029. DEHYDROQUINASE_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AROQ_ACTPL

Accession

Primary (citable) accession number: P43877

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	September 22, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)