P58687 (AROD_SALTY) 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:	STM1358

Organism

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

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

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. Ref.3 Ref.4
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.3 Ref.4
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 Reference 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_0000138806

Regions

Region

46 – 48

3

Substrate binding HAMAP-Rule MF_00214

Sites

Active site

143

1

Proton donor/acceptor Ref.2 Ref.3 Ref.4

Active site

170

1

Schiff-base intermediate with substrate Ref.2 Ref.3 Ref.4

Binding site

82

1

Substrate

Binding site

213

1

Substrate

Binding site

232

1

Substrate

Binding site

236

1

Substrate

Experimental info

Mutagenesis

170

1

K → M: Abolishes enzyme activity. Ref.4

Mutagenesis

232

1

S → A: Reduces enzyme activity 50-fold. Ref.3

Mutagenesis

236

1

Q → A: Nearly abolishes enzyme activity. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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

Helix

207 – 210

4

Helix

211 – 214

4

Helix

216 – 219

4

Beta strand

223 – 225

3

Beta strand

227 – 229

3

Helix

239 – 251

13

Sequences

	Sequence		Length	Mass (Da)
	P58687 [UniParc]. Last modified January 31, 2002. Version 1. Checksum: 10BB561E38EA0A75	FASTA	252	27,325
	10 20 30 40 50 60 MKTVTVRDLV VGEGAPKIIV SLMGKTITDV KSEALAYREA DFDILEWRVD HFANVTTAES 70 80 90 100 110 120 VLEAAGAIRE IITDKPLLFT FRSAKEGGEQ ALTTGQYIDL NRAAVDSGLV DMIDLELFTG 130 140 150 160 170 180 DDEVKATVGY AHQHNVAVIM SNHDFHKTPA AEEIVQRLRK MQELGADIPK IAVMPQTKAD 190 200 210 220 230 240 VLTLLTATVE MQERYADRPI ITMSMSKTGV ISRLAGEVFG SAATFGAVKK ASAPGQISVA 250 DLRTVLTILH QA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[2]	"New insights into the mechanism of the Schiff base hydrolysis catalyzed by type I dehydroquinate dehydratase from S. enterica: a theoretical study." Yao Y., Li Z.S. Org. Biomol. Chem. 10:7037-7044(2012) [PubMed] [Europe PMC] [Abstract] Cited for: ACTIVE SITE.
[3]	"A conserved surface loop in type I dehydroquinate dehydratases positions an active site arginine and functions in substrate binding." Light S.H., Minasov G., Shuvalova L., Peterson S.N., Caffrey M., Anderson W.F., Lavie A. Biochemistry 50:2357-2363(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.03 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF SER-232 AND GLN-236.
[4]	"Insights into the mechanism of type I dehydroquinate dehydratases from structures of reaction intermediates." Light S.H., Minasov G., Shuvalova L., Duban M.E., Caffrey M., Anderson W.F., Lavie A. J. Biol. Chem. 286:3531-3539(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF WILD-TYPE AND MUTANT MET-170 IN COMPLEX WITH 3-DEHYDROQUINIC ACID, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF LYS-170.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE006468 Genomic DNA. Translation: AAL20283.1.

RefSeq

NP_460324.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3L2I	X-ray	1.85	A/B	1-252	[»]
3LB0	X-ray	1.65	A/B	1-252	[»]
3M7W	X-ray	1.95	A/B/C/D/E/F	1-252	[»]
3NNT	X-ray	1.60	A/B	1-252	[»]
3O1N	X-ray	1.03	A/B	1-252	[»]
3OEX	X-ray	1.90	A/B/C/D	1-252	[»]
3S42	X-ray	1.45	A/B	1-252	[»]
4GFS	X-ray	1.80	A/B	1-252	[»]
4GUF	X-ray	1.50	A/B	1-252	[»]
4GUG	X-ray	1.62	A/B	1-252	[»]
4GUH	X-ray	1.95	A/B	1-252	[»]
4GUI	X-ray	1.78	A/B	1-252	[»]
4GUJ	X-ray	1.50	A/B	1-252	[»]
4IUO	X-ray	1.80	A/B	1-252	[»]

ProteinModelPortal

P58687.

SMR

P58687. Positions 1-252.

ModBase

Search...

Protein-protein interaction databases

STRING

99287.STM1358.

Proteomic databases

PRIDE

P58687.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAL20283; AAL20283; STM1358.

GeneID

1252876.

KEGG

stm:STM1358.

PATRIC

32381199. VBISalEnt20916_1442.

Phylogenomic databases

HOGENOM

HOG000105514.

KO

K03785.

OMA

IIEWRVD.

ProtClustDB

PRK02412.

Enzyme and pathway databases

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

P58687.

Entry information

Entry name

AROD_SALTY

Accession

Primary (citable) accession number: P58687

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 31, 2002
Last sequence update:	January 31, 2002
Last modified:	May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program