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Protein

Shikimate dehydrogenase (NADP(+))

Gene

aroE

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).UniRule annotation

Catalytic activityi

Shikimate + NADP+ = 3-dehydroshikimate + NADPH.UniRule annotation

Pathwayi: chorismate biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.UniRule 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. 3-dehydroquinate dehydratase (aroQ)
  4. Shikimate dehydrogenase (NADP(+)) (aroE)
  5. Shikimate kinase (aroK)
  6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
  7. Chorismate synthase (aroC)
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
Binding sitei60 – 601ShikimateUniRule annotation1 Publication
Active sitei64 – 641Proton acceptorUniRule annotation1 Publication
Binding sitei85 – 851ShikimateUniRule annotation1 Publication
Binding sitei100 – 1001ShikimateUniRule annotation1 Publication
Binding sitei205 – 2051NADP; via carbonyl oxygenUniRule annotation1 Publication
Binding sitei207 – 2071ShikimateUniRule annotation1 Publication
Binding sitei228 – 2281NADP; via carbonyl oxygenUniRule annotation1 Publication
Binding sitei235 – 2351ShikimateUniRule annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi123 – 1275NADPUniRule annotation1 Publication
Nucleotide bindingi146 – 1516NADPUniRule annotation1 Publication

GO - Molecular functioni

  • NADP binding Source: UniProtKB
  • shikimate 3-dehydrogenase (NADP+) activity Source: UniProtKB-HAMAP

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1082-MONOMER.
BRENDAi1.1.1.25. 2305.
UniPathwayiUPA00053; UER00087.

Names & Taxonomyi

Protein namesi
Recommended name:
Shikimate dehydrogenase (NADP(+))UniRule annotation (EC:1.1.1.25UniRule annotation)
Short name:
SDHUniRule annotation
Gene namesi
Name:aroEUniRule annotation
Ordered Locus Names:TTHA1050
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263Shikimate dehydrogenase (NADP(+))PRO_1000078133Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi300852.TTHA1050.

Structurei

Secondary structure

1
263
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 109Combined sources
Helixi16 – 2611Combined sources
Beta strandi31 – 377Combined sources
Helixi40 – 423Combined sources
Helixi43 – 5311Combined sources
Beta strandi55 – 595Combined sources
Turni61 – 655Combined sources
Helixi66 – 705Combined sources
Beta strandi72 – 743Combined sources
Helixi76 – 816Combined sources
Beta strandi86 – 905Combined sources
Beta strandi93 – 975Combined sources
Helixi100 – 11011Combined sources
Beta strandi119 – 1224Combined sources
Helixi126 – 13712Combined sources
Beta strandi142 – 1454Combined sources
Helixi149 – 15911Combined sources
Helixi166 – 1716Combined sources
Beta strandi173 – 1775Combined sources
Turni181 – 1844Combined sources
Helixi193 – 1953Combined sources
Beta strandi198 – 2058Combined sources
Beta strandi208 – 2114Combined sources
Helixi213 – 2208Combined sources
Beta strandi224 – 2263Combined sources
Helixi229 – 24416Combined sources
Helixi250 – 26011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WXDX-ray2.10A/B1-263[»]
2CY0X-ray1.90A/B1-263[»]
2D5CX-ray1.65A/B1-263[»]
2EV9X-ray1.90A/B1-263[»]
ProteinModelPortaliQ5SJF8.
SMRiQ5SJF8. Positions 1-263.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SJF8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 163Shikimate bindingUniRule annotation1 Publication

Sequence similaritiesi

Belongs to the shikimate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105E2X. Bacteria.
COG0169. LUCA.
HOGENOMiHOG000237875.
KOiK00014.
OMAiSIYIDAT.
OrthoDBiEOG64R67G.
PhylomeDBiQ5SJF8.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00222. Shikimate_DH_AroE.
InterProiIPR016040. NAD(P)-bd_dom.
IPR011342. Shikimate_DH.
IPR013708. Shikimate_DH-bd_N.
IPR022893. Shikimate_DH_fam.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF01488. Shikimate_DH. 1 hit.
PF08501. Shikimate_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00507. aroE. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5SJF8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRFAVLGHP VAHSLSPAMH AFALESLGLE GSYEAWDTPL EALPGRLKEV
60 70 80 90 100
RRAFRGVNLT LPLKEAALAH LDWVSPEAQR IGAVNTVLQV EGRLFGFNTD
110 120 130 140 150
APGFLEALKA GGIPLKGPAL VLGAGGAGRA VAFALREAGL EVWVWNRTPQ
160 170 180 190 200
RALALAEEFG LRAVPLEKAR EARLLVNATR VGLEDPSASP LPAELFPEEG
210 220 230 240 250
AAVDLVYRPL WTRFLREAKA KGLKVQTGLP MLAWQGALAF RLWTGLLPDP
260
SGMEEAARRA LGV
Length:263
Mass (Da):28,284
Last modified:December 21, 2004 - v1
Checksum:iBF53F1D49A1A82A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70873.1.
RefSeqiWP_011228401.1. NC_006461.1.
YP_144316.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70873; BAD70873; BAD70873.
GeneIDi3169915.
KEGGittj:TTHA1050.
PATRICi23957060. VBITheThe93045_1030.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70873.1.
RefSeqiWP_011228401.1. NC_006461.1.
YP_144316.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WXDX-ray2.10A/B1-263[»]
2CY0X-ray1.90A/B1-263[»]
2D5CX-ray1.65A/B1-263[»]
2EV9X-ray1.90A/B1-263[»]
ProteinModelPortaliQ5SJF8.
SMRiQ5SJF8. Positions 1-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1050.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70873; BAD70873; BAD70873.
GeneIDi3169915.
KEGGittj:TTHA1050.
PATRICi23957060. VBITheThe93045_1030.

Phylogenomic databases

eggNOGiENOG4105E2X. Bacteria.
COG0169. LUCA.
HOGENOMiHOG000237875.
KOiK00014.
OMAiSIYIDAT.
OrthoDBiEOG64R67G.
PhylomeDBiQ5SJF8.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00087.
BioCyciTTHE300852:GH8R-1082-MONOMER.
BRENDAi1.1.1.25. 2305.

Miscellaneous databases

EvolutionaryTraceiQ5SJF8.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00222. Shikimate_DH_AroE.
InterProiIPR016040. NAD(P)-bd_dom.
IPR011342. Shikimate_DH.
IPR013708. Shikimate_DH-bd_N.
IPR022893. Shikimate_DH_fam.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF01488. Shikimate_DH. 1 hit.
PF08501. Shikimate_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00507. aroE. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  2. "Crystal structures of shikimate dehydrogenase AroE from Thermus thermophilus HB8 and its cofactor and substrate complexes: insights into the enzymatic mechanism."
    Bagautdinov B., Kunishima N.
    J. Mol. Biol. 373:424-438(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH SHIKIMATE AND NADP, REACTION MECHANISM, ACTIVE SITE, SUBUNIT.
    Strain: HB8 / ATCC 27634 / DSM 579.

Entry informationi

Entry nameiAROE_THET8
AccessioniPrimary (citable) accession number: Q5SJF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 21, 2004
Last modified: December 9, 2015
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.