3-dehydroquinate synthase - Thermus thermophilus

Preferred order of sections

Names and origin

Protein names

Recommended name:
3-dehydroquinate synthase HAMAP-Rule MF_00110
EC=4.2.3.4 HAMAP-Rule MF_00110

Gene names

Name:

aroB HAMAP-Rule MF_00110

Organism

Thermus thermophilus PDB 1UJN

Taxonomic identifier

274 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate. HAMAP-Rule MF_00110 SAAS SAAS016037
Cofactor	Divalent metal cations By similarity. HAMAP-Rule MF_00110 SAAS SAAS016037 NAD By similarity. HAMAP-Rule MF_00110 SAAS SAAS016037
Pathway	Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. HAMAP-Rule MF_00110 SAAS SAAS016037
Subunit structure	Monomer By similarity. HAMAP-Rule MF_00110 SAAS SAAS016037
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00110.
Sequence similarities	Belongs to the dehydroquinate synthase family. HAMAP-Rule MF_00110

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis HAMAP-Rule MF_00110 SAAS SAAS016037
Cellular component	Cytoplasm HAMAP-Rule MF_00110 SAAS SAAS016037
Ligand	NAD HAMAP-Rule MF_00110 SAAS SAAS016037
Molecular function	Lyase HAMAP-Rule MF_00110
Technical term	3D-structure PDB 1UJN
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
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	3-dehydroquinate synthase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Active site

131

1

Proton donor/acceptor PDB 1UJN

Active site

220

1

Proton donor/acceptor PDB 1UJN

Active site

235

1

Proton donor/acceptor PDB 1UJN

Site

109

1

Important for catalytic activity PDB 1UJN

Site

210

1

Important for catalytic activity PDB 1UJN

Site

224

1

Important for catalytic activity PDB 1UJN

Site

228

1

Important for catalytic activity PDB 1UJN

Sequences

Sequence

Length

Mass (Da)

Tools

P83703 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 642813E920F4880F
Show »

FASTA

348

37,510

        10         20         30         40         50         60 
MQRLEVREPV PYPILVGEGV LKEVPPLAGP AALLFDRRVE GFAQEVAKAL GVRHLLGLPG 

        70         80         90        100        110        120 
GEAAKSLEVY GKVLSWLAEK GLPRNATLLV VGGGTLTDLG GFVAATYLRG VAYLAFPTTT 

       130        140        150        160        170        180 
LAIVDASVGG KTGINLPEGK NLVGAFHFPQ GVYAELRALK TLPLPTFKEG LVEAFKHGLI 

       190        200        210        220        230        240 
AGDEALLKVE DLTPQSPRLE AFLARAVAVK VRVTEEDPLE KGKRRLLNLG HTLGHALEAQ 

       250        260        270        280        290        300 
TRHALPHGMA VAYGLLYAAL LGRALGGEDL LPPVRRLLLW LSPPPLPPLA FEDLLPYLLR 

       310        320        330        340 
DKKKVSESLH WVVPLAPGRL VVRPLPEGLL REAFAAWREE LKGLGLLR

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References

[1]

"Crystal structure of dehydroquinate synthase from Thermus thermophilus HB8 showing functional importance of the dimeric state."
Sugahara M., Nodake Y., Sugahara M., Kunishima N.
Proteins 58:249-252(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), ACTIVE SITE.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UJN	X-ray	1.80	A/B	1-348	[»]

ProteinModelPortal

P83703.

SMR

P83703. Positions 1-347.

ModBase

Search...

Protein-protein interaction databases

STRING

262724.TTC1020.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00053; UER00085.

Family and domain databases

HAMAP

MF_00110. DHQ_synthase.

InterPro

IPR016037. DHQ_synth_AroB.
[Graphical view]

PIRSF

PIRSF001455. DHQ_synth. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P83703.

Entry information

Entry name

P83703_THETH

Accession

Primary (citable) accession number: P83703

Entry history

Integrated into UniProtKB/TrEMBL:	December 15, 2003
Last sequence update:	December 15, 2003
Last modified:	April 3, 2013
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)