Reviewed, UniProtKB/Swiss-Prot P0A4Z6 (AROQ_MYCTU)

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
Synonyms:	aroD
Ordered Locus Names:	Rv2537c, MT2612
ORF Names:	MTCY159.19

Organism

Mycobacterium tuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.4
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 Complete proteome
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

Initiator methionine

1

1

Removed HAMAP MF_00169

Chain

2 – 147

146

3-dehydroquinate dehydratase HAMAP MF_00169

PRO_0000159910

Regions

Region

103 – 104

2

Substrate binding HAMAP MF_00169

Sites

Active site

25

1

Proton acceptor HAMAP MF_00169

Active site

102

1

Proton donor HAMAP MF_00169

Binding site

76

1

Substrate HAMAP MF_00169

Binding site

82

1

Substrate HAMAP MF_00169

Binding site

89

1

Substrate HAMAP MF_00169

Binding site

113

1

Substrate HAMAP MF_00169

Site

20

1

Transition state stabilizer HAMAP MF_00169

Experimental info

Sequence conflict

117

1

Y → I in CAA42096. Ref.1

Secondary structure

1

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147

Helix Strand Turn

Details...

Beta strand

5 – 10

6

Helix

14 – 16

3

Turn

17 – 19

3

Helix

30 – 43

14

Beta strand

47 – 52

6

Helix

56 – 69

14

Beta strand

73 – 76

4

Helix

78 – 82

5

Helix

85 – 92

8

Beta strand

98 – 104

7

Helix

106 – 108

3

Helix

111 – 114

4

Helix

119 – 121

3

Beta strand

122 – 129

8

Helix

132 – 143

12

Sequences

	Sequence		Length	Mass (Da)
	P0A4Z6-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 9EE0E1B14B4DB5F6	FASTA	147	15,790
	10 20 30 40 50 60 MSELIVNVIN GPNLGRLGRR EPAVYGGTTH DELVALIERE AAELGLKAVV RQSDSEAQLL 70 80 90 100 110 120 DWIHQAADAA EPVILNAGGL THTSVALRDA CAELSAPLIE VHISNVHARE EFRRHSYLSP 130 140 IATGVIVGLG IQGYLLALRY LAEHVGT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Mycobacterium tuberculosis shikimate pathway genes: evolutionary relationship between biosynthetic and catabolic 3-dehydroquinases." Garbe T., Servos S., Hawkins A., Dimitriadis G., Young D., Dougan G., Charles I.G. Mol. Gen. Genet. 228:385-392(1991) [PubMed: 1910148] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[3]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[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: 10360352] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT.
[5]	"Specificity of substrate recognition by type II dehydroquinases as revealed by binding of polyanions." Evans L.D., Roszak A.W., Noble L.J., Robinson D.A., Chalk P.A., Matthews J.L., Coggins J.R., Price N.C., Lapthorn A.J. FEBS Lett. 530:24-30(2002) [PubMed: 12387860] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH POLYANION.
[6]	"Structural basis for specificity of oxime based inhibitors towards type II dehydroquinase from Mycobacterium tuberculosis." Robinson D.A., Roszak A.W., Frederickson M., Abell C., Coggins J.R., Lapthorn A.J. Submitted (MAY-2004) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X59509 Genomic DNA. Translation: CAA42096.1.
BX842580 Genomic DNA. Translation: CAB06171.1.
AE000516 Genomic DNA. Translation: AAK46922.1.

PIR

E70658.

RefSeq

NP_217053.1.
NP_337108.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H05	X-ray	1.50	A	2-147	[»]
1H0R	X-ray	2.10	A	2-147	[»]
1H0S	X-ray	1.70	A	2-147	[»]
2DHQ	X-ray	2.00	A	2-147	[»]

ModBase

Search...

Genome annotation databases

GeneID

888397.
925700.

GenomeReviews

Gene locus MT2612 in contig AE000516_GR.
Gene locus Rv2537c in contig AL123456_GR.

KEGG

mtc:MT2612.
mtu:Rv2537c.

TIGR

MT2612.

Organism-specific databases

TubercuList

Rv2537c.

Phylogenomic databases

HOGENOM

P0A4Z6.

OMA

EPGIYGG.

Enzyme and pathway databases

BRENDA

4.2.1.10. 809.

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_MYCTU

Accession

Primary (citable) accession number: P0A4Z6
Secondary accession number(s): P36918, P95016

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 37 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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