Reviewed, UniProtKB/Swiss-Prot Q9X5C9 (AROE_CORGL)

Names and origin

Protein names

Recommended name:
    Quinate/shikimate dehydrogenase
    EC=1.1.1.24
    EC=1.1.1.-
Alternative name(s):
    NAD(+)-dependent quinate dehydrogenase
      Short name=QDH
      Short name=CglQDH

Gene names

Name:	aroE
Ordered Locus Names:	Cgl0424, cg0504

Organism

Corynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP]

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	283 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the NAD+-dependent oxidation of both quinate and shikimate to 3-dehydroquinate and 3-dehydroshikimate, respectively. Seems to play a key role in the quinate degradation pathway. Ref.4
Catalytic activity	Quinate + NAD+ = 3-dehydroquinate + NADH. HAMAP MF_00222 Shikimate + NAD+ = 3-dehydroshikimate + NADH. HAMAP MF_00222
Pathway	Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. HAMAP MF_00222
Subunit structure	Homodimer. Ref.4
Miscellaneous	Has a different substrate and cosubstrate specificities relative to all other known bacterial shikimate/quinate dehydrogenases. HAMAP MF_00222
Sequence similarities	Belongs to the shikimate dehydrogenase family.
Biophysicochemical properties	Kinetic parameters: The catalytic efficiency with quinate is 3.3-fold higher than that with shikimate. With NADP+ instead of NAD+ as cosubstrate, activity decreases by more than 300-fold with either shikimate or quinate as a substrate. KM=10.2 mM for quinate HAMAP MF_00222 KM=46.6 mM for shikimate pH dependence: Optimum pH is 9-10.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	binding Inferred from electronic annotation. Source: InterPro quinate 5-dehydrogenase activity Inferred from electronic annotation. Source: EC shikimate 5-dehydrogenase 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 – 283

283

Quinate/shikimate dehydrogenase HAMAP MF_00222

PRO_0000136001

Regions

Nucleotide binding

134 – 138

5

NAD By similarity

Nucleotide binding

251 – 255

5

NAD By similarity

Sites

Active site

73

1

Proton acceptor Potential

Binding site

110

1

Substrate By similarity

Binding site

158

1

NAD Probable

Experimental info

Sequence conflict

29

1

A → P in AAD30993. Ref.1

Sequence conflict

135 – 143

9

AGGVGNAVA → RRRRKRSR in AAD30993. Ref.1

Sequence conflict

211

1

Missing in AAD30993. Ref.1

Sequence conflict

272 – 273

2

DV → T in AAD30993. Ref.1

Secondary structure

1

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283

Helix Strand Turn

Details...

Beta strand

5 – 13

9

Helix

19 – 29

11

Beta strand

34 – 40

7

Turn

44 – 48

5

Helix

51 – 60

10

Beta strand

65 – 68

4

Turn

73 – 76

4

Helix

77 – 79

3

Beta strand

80 – 83

4

Helix

85 – 90

6

Beta strand

95 – 98

4

Beta strand

104 – 107

4

Helix

109 – 121

13

Beta strand

128 – 133

6

Helix

139 – 148

10

Beta strand

152 – 160

9

Helix

161 – 175

15

Beta strand

180 – 185

6

Helix

188 – 194

7

Beta strand

195 – 200

6

Helix

216 – 218

3

Beta strand

224 – 228

5

Beta strand

231 – 234

4

Helix

236 – 244

9

Beta strand

247 – 249

3

Helix

252 – 267

16

Helix

273 – 281

9

Sequences

	Sequence		Length	Mass (Da)
	Q9X5C9-1 [UniParc]. Last modified July 26, 2002. Version 2. Checksum: 2DBCE25D186DAF74	FASTA	283	29,697
	10 20 30 40 50 60 MNDSILLGLI GQGLDLSRTP AMHEAEGLAQ GRATVYRRID TLGSRASGQD LKTLLDAALY 70 80 90 100 110 120 LGFNGLNITH PYKQAVLPLL DEVSEQATQL GAVNTVVIDA TGHTTGHNTD VSGFGRGMEE 130 140 150 160 170 180 GLPNAKLDSV VQVGAGGVGN AVAYALVTHG VQKLQVADLD TSRAQALADV INNAVGREAV 190 200 210 220 230 240 VGVDARGIED VIAAADGVVN ATPMGMPAHP GTAFDVSCLT KDHWVGDVVY MPIETELLKA 250 260 270 280 ARALGCETLD GTRMAIHQAV DAFRLFTGLE PDVSRMRETF LSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The cloning and phylogenetic analysis of the 3-dehydroquinase gene from Corynebacterium glutamicum." Joy J., O'Donohue M., Dunican L.K. Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613.
[2]	"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]	"1.6 Angstroms structure of an NAD(+)-dependent quinate dehydrogenase from Corynebacterium glutamicum." Schoepe J., Niefind K., Schomburg D. Acta Crystallogr. D 64:803-809(2008) [PubMed: 18566515] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, REACTION MECHANISM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF124518 Genomic DNA. Translation: AAD30993.1.
BA000036 Genomic DNA. Translation: BAB97817.1.
BX927149 Genomic DNA. Translation: CAF19140.1.

RefSeq

NP_599671.1.
YP_224726.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2NLO	X-ray	1.64	A	1-283	[»]

ModBase

Search...

Genome annotation databases

GeneID

1021203.
3343183.

GenomeReviews

Gene locus Cgl0424 in contig BA000036_GR.

KEGG

cgb:cg0504.
cgl:NCgl0409.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HBG553408.

OMA

GFNGLNI.

Enzyme and pathway databases

BioCyc

CGLU196627:CG0504-MONOMER.

BRENDA

1.1.1.25. 812.

Family and domain databases

HAMAP

MF_00222. Shikimate_DH_AroE. Divergent sequence.
[Tree]

InterPro

IPR016040. NAD(P)-bd_dom.
IPR013708. Shikimate_DH-bd_N.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

PF01488. Shikimate_DH. 1 hit.
PF08501. Shikimate_dh_N. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AROE_CORGL

Accession

Primary (citable) accession number: Q9X5C9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	July 26, 2002
Last modified:	February 9, 2010
This is version 74 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)