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Protein

3-dehydroquinate synthase

Gene

aroB

Organism
Thermus thermophilus
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate.UniRule annotationSAAS annotation

Cofactori

Protein has several cofactor binding sites:
  • Co2+UniRule annotation, Zn2+UniRule annotationNote: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn2+.UniRule annotation
  • Co2+, Zn2+Note: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn2+.
  • NAD(+)UniRule annotationSAAS annotation

Pathway: chorismate biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.UniRule annotationSAAS annotation
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. 3-dehydroquinate synthase (aroB)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. no protein annotated in this organism
  7. no protein annotated in this organism
This subpathway is part of the pathway chorismate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate, the pathway chorismate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei109 – 1091Important for catalytic activityCombined sources
Active sitei131 – 1311Proton donor/acceptorCombined sources
Sitei210 – 2101Important for catalytic activityCombined sources
Active sitei220 – 2201Proton donor/acceptorCombined sources
Sitei224 – 2241Important for catalytic activityCombined sources
Sitei228 – 2281Important for catalytic activityCombined sources
Active sitei235 – 2351Proton donor/acceptorCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationSAAS annotation

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesisUniRule annotationSAAS annotation

Keywords - Ligandi

CobaltUniRule annotationSAAS annotation, NADUniRule annotationSAAS annotation, ZincUniRule annotationSAAS annotation

Enzyme and pathway databases

BRENDAi4.2.3.4. 2305.
UniPathwayiUPA00053; UER00085.

Names & Taxonomyi

Protein namesi
Recommended name:
3-dehydroquinate synthaseUniRule annotationSAAS annotation (EC:4.2.3.4UniRule annotationSAAS annotation)
Gene namesi
Name:aroBUniRule annotation
OrganismiThermus thermophilusImported
Taxonomic identifieri274 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Interactioni

Subunit structurei

Monomer.UniRule annotationSAAS annotation

Protein-protein interaction databases

STRINGi262724.TTC1020.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UJNX-ray1.80A/B1-348[»]
ProteinModelPortaliP83703.
SMRiP83703. Positions 1-347.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83703.

Family & Domainsi

Sequence similaritiesi

Belongs to the dehydroquinate synthase family.UniRule annotation

Family and domain databases

HAMAPiMF_00110. DHQ_synthase.
InterProiIPR016037. DHQ_synth_AroB.
IPR030963. DHQ_synth_fam.
IPR030960. DHQS/DOIS.
[Graphical view]
PfamiPF01761. DHQ_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF001455. DHQ_synth. 1 hit.

Sequencei

Sequence statusi: Complete.

P83703-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRLEVREPV PYPILVGEGV LKEVPPLAGP AALLFDRRVE GFAQEVAKAL
60 70 80 90 100
GVRHLLGLPG GEAAKSLEVY GKVLSWLAEK GLPRNATLLV VGGGTLTDLG
110 120 130 140 150
GFVAATYLRG VAYLAFPTTT LAIVDASVGG KTGINLPEGK NLVGAFHFPQ
160 170 180 190 200
GVYAELRALK TLPLPTFKEG LVEAFKHGLI AGDEALLKVE DLTPQSPRLE
210 220 230 240 250
AFLARAVAVK VRVTEEDPLE KGKRRLLNLG HTLGHALEAQ TRHALPHGMA
260 270 280 290 300
VAYGLLYAAL LGRALGGEDL LPPVRRLLLW LSPPPLPPLA FEDLLPYLLR
310 320 330 340
DKKKVSESLH WVVPLAPGRL VVRPLPEGLL REAFAAWREE LKGLGLLR
Length:348
Mass (Da):37,510
Last modified:December 15, 2003 - v1
Checksum:i642813E920F4880F
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UJNX-ray1.80A/B1-348[»]
ProteinModelPortaliP83703.
SMRiP83703. Positions 1-347.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262724.TTC1020.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00053; UER00085.
BRENDAi4.2.3.4. 2305.

Miscellaneous databases

EvolutionaryTraceiP83703.

Family and domain databases

HAMAPiMF_00110. DHQ_synthase.
InterProiIPR016037. DHQ_synth_AroB.
IPR030963. DHQ_synth_fam.
IPR030960. DHQS/DOIS.
[Graphical view]
PfamiPF01761. DHQ_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF001455. DHQ_synth. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiP83703_THETH
AccessioniPrimary (citable) accession number: P83703
Entry historyi
Integrated into UniProtKB/TrEMBL: December 15, 2003
Last sequence update: December 15, 2003
Last modified: June 24, 2015
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sourcesImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.