P24670 (AROD_SALTI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-dehydroquinate dehydratase
Short name=3-dehydroquinase
EC=4.2.1.10

Alternative name(s):
Type I DHQase

Gene names

Name:	aroD
Ordered Locus Names:	STY1760, t1231

Organism

Salmonella typhi [Complete proteome] [HAMAP]

Taxonomic identifier

90370 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I

Protein attributes

Sequence length	252 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	3-dehydroquinate = 3-dehydroshikimate + H2O. HAMAP-Rule MF_00214
Pathway	Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. HAMAP-Rule MF_00214
Subunit structure	Homodimer. Ref.4 Ref.5
Sequence similarities	Belongs to the type-I 3-dehydroquinase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Ligand	Schiff base
Molecular function	Lyase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: HAMAP chorismate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
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 – 252

252

3-dehydroquinate dehydratase HAMAP-Rule MF_00214

PRO_0000138805

Regions

Region

46 – 48

3

Substrate binding HAMAP-Rule MF_00214

Sites

Active site

143

1

Proton donor/acceptor Ref.4 Ref.5

Active site

170

1

Schiff-base intermediate with substrate Ref.4 Ref.5

Binding site

82

1

Substrate

Binding site

213

1

Substrate

Binding site

232

1

Substrate

Binding site

236

1

Substrate

Experimental info

Sequence conflict

156

1

L → S in CAA38418. Ref.1

Secondary structure

1

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252

Helix Strand Turn

Details...

Beta strand

4 – 6

3

Beta strand

9 – 11

3

Beta strand

13 – 15

3

Beta strand

17 – 22

6

Helix

27 – 37

11

Beta strand

43 – 48

6

Helix

49 – 51

3

Turn

53 – 56

4

Helix

58 – 71

14

Beta strand

77 – 80

4

Helix

84 – 86

3

Helix

94 – 107

14

Beta strand

111 – 116

6

Helix

117 – 119

3

Helix

121 – 133

13

Beta strand

137 – 146

10

Helix

151 – 163

13

Beta strand

167 – 173

7

Helix

178 – 194

17

Beta strand

201 – 204

4

Turn

206 – 209

4

Helix

210 – 214

5

Helix

216 – 219

4

Beta strand

223 – 225

3

Beta strand

227 – 230

4

Helix

239 – 250

12

Sequences

	Sequence		Length	Mass (Da)
	P24670 [UniParc]. Last modified December 5, 2001. Version 2. Checksum: F9D4D4C86D18F17B	FASTA	252	27,649
	10 20 30 40 50 60 MKTVTVKNLI IGEGMPKIIV SLMGRDINSV KAEALAYREA TFDILEWRVD HFMDIASTQS 70 80 90 100 110 120 VLTAARVIRD AMPDIPLLFT FRSAKEGGEQ TITTQHYLTL NRAAIDSGLV DMIDLELFTG 130 140 150 160 170 180 DADVKATVDY AHAHNVYVVM SNHDFHQTPS AEEMVLRLRK MQALGADIPK IAVMPQSKHD 190 200 210 220 230 240 VLTLLTATLE MQQHYADRPV ITMSMAKEGV ISRLAGEVFG SAATFGAVKQ ASAPGQIAVN 250 DLRSVLMILH NA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of the aroD gene encoding 3-dehydroquinase from Salmonella typhi." Servos S., Chatfield S., Hone D., Levine M., Dimitriadis G., Pickard D., Dougan G., Fairweather N., Charles I.G. J. Gen. Microbiol. 137:147-152(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 700931 / Ty2.
[2]	"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18." Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. , Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G. Nature 413:848-852(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CT18.
[3]	"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18." Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R. J. Bacteriol. 185:2330-2337(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700931 / Ty2.
[4]	"The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction." Gourley D.G., Shrive A.K., Polikarpov I., Krell T., Coggins J.R., Hawkins A.R., Isaacs N.W., Sawyer L. Nat. Struct. Biol. 6:521-525(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH 3-DEHYDROQUINATE, SUBUNIT, ACTIVE SITE.
[5]	"Comparison of different crystal forms of 3-dehydroquinase from Salmonella typhi and its implication for the enzyme activity." Lee W.H., Perles L.A., Nagem R.A., Shrive A.K., Hawkins A., Sawyer L., Polikarpov I. Acta Crystallogr. D 58:798-804(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) IN COMPLEX WITH 3-DEHYDROSHIKIMATE, ACTIVE SITE, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X54546 Genomic DNA. Translation: CAA38418.1.
AL627271 Genomic DNA. Translation: CAD02002.1.
AE014613 Genomic DNA. Translation: AAO68886.1.

PIR

S15652.

RefSeq

NP_805037.1. NC_004631.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GQN	X-ray	1.78	A	1-252	[»]
1L9W	X-ray	2.10	A/B/C/D	1-252	[»]
1QFE	X-ray	2.10	A/B	1-252	[»]

ProteinModelPortal

P24670.

SMR

P24670. Positions 1-252.

ModBase

Search...

Protein-protein interaction databases

STRING

220341.STY1760.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAO68886; AAO68886; t1231.
CAD02002; CAD02002; CAD02002.

GeneID

1070649.

KEGG

stt:t1231.

PATRIC

18541418. VBISalEnt120419_1771.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0710.

HOGENOM

HOG000105514.

KO

K03785.

OMA

IIEWRVD.

ProtClustDB

PRK02412.

Enzyme and pathway databases

SABIO-RK

P24670.

UniPathway

UPA00053; UER00086.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

HAMAP

MF_00214. AroD.

InterPro

IPR018508. 3-dehydroquinate_DH_AS.
IPR013785. Aldolase_TIM.
IPR001381. DHquinase_I.
[Graphical view]

Pfam

PF01487. DHquinase_I. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01093. aroD. 1 hit.

PROSITE

PS01028. DEHYDROQUINASE_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P24670.

Entry information

Entry name

AROD_SALTI

Accession

Primary (citable) accession number: P24670

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	December 5, 2001
Last modified:	May 1, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program