P54517 (AROQ_BACSU) 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 II DHQase

Gene names

Name:	yqhS
Ordered Locus Names:	BSU24470

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	148 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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.3
Sequence similarities	Belongs to the type-II 3-dehydroquinase family.
Caution	Phe-23 is present instead of the conserved Tyr which is expected to be an active site residue.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
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: UniProtKB-KW
Molecular function	3-dehydroquinate dehydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 148

148

3-dehydroquinate dehydratase HAMAP MF_00169

PRO_0000159872

Regions

Region

101 – 102

2

Substrate binding By similarity

Sites

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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148

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Helix

12 – 14

3

Helix

20 – 23

4

Helix

28 – 42

15

Beta strand

45 – 50

6

Helix

54 – 64

11

Turn

65 – 67

3

Beta strand

69 – 74

6

Helix

76 – 80

5

Helix

83 – 90

8

Beta strand

96 – 102

7

Helix

104 – 106

3

Helix

109 – 112

4

Helix

117 – 119

3

Beta strand

120 – 127

8

Helix

130 – 140

11

Sequences

	Sequence		Length	Mass (Da)
	P54517 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 71B253931B43EFE7	FASTA	148	16,431
	10 20 30 40 50 60 MPHFLILNGP NVNRLGSREP EVFGRQTLTD IETDLFQFAE ALHIQLTFFQ SNHEGDLIDA 70 80 90 100 110 120 IHEAEEQYSG IVLNPGALSH YSYAIRDAVS SISLPVVEVH LSNLYAREEF RHQSVIAPVA 130 140 KGQIVGLGAE GYKLAVRYLL SQQGGESR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes." Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y. Microbiology 142:3103-3111(1996) [PubMed: 8969508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / JH642.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Crystal structure of the type II dehydroquinase from Bacillus subtilis." Robinson D.A., Roszak A.W., Coggins J.R., Lapthorn A.J. Submitted (NOV-2001) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-144, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D84432 Genomic DNA. Translation: BAA12556.1.
AL009126 Genomic DNA. Translation: CAB14378.1.

PIR

B69960.

RefSeq

NP_390327.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GQO	X-ray	2.10	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/X/Y	2-144	[»]

ProteinModelPortal

P54517.

SMR

P54517. Positions 2-144.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000002358; EBBACP00000002358; EBBACG00000002353.

GeneID

938557.

GenomeReviews

Gene locus BSU24470 in contig AL009126_GR.

KEGG

bsu:BSU24470.

NMPDR

fig|224308.1.peg.2451.

PATRIC

18976728. VBIBacSub10457_2554.

Organism-specific databases

GenoList

BSU24470.

Phylogenomic databases

GeneTree

EBGT00050000003572.

HOGENOM

HBG284657.

OMA

VDWLHEA.

PhylomeDB

P54517.

ProtClustDB

PRK05395.

Enzyme and pathway databases

BioCyc

BSUB:BSU24470-MONOMER.

Family and domain databases

HAMAP

MF_00169. AroQ.
[Tree]

InterPro

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

Gene3D

G3DSA:3.40.50.9100. DHquinase_II. 1 hit.

KO

K03786.

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]

SUPFAM

SSF52304. DHquinase_II. 1 hit.

TIGRFAMs

TIGR01088. AroQ. 1 hit.

PROSITE

PS01029. DEHYDROQUINASE_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AROQ_BACSU

Accession

Primary (citable) accession number: P54517

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program