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Protein

Shikimate dehydrogenase (NADP(+))

Gene

aroE

Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Status
Reviewed-Annotation score: Annotation score: 4 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei65 – 651ShikimateUniRule annotation3 Publications
Active sitei69 – 691Proton acceptorUniRule annotation2 Publications
Binding sitei90 – 901ShikimateUniRule annotation2 Publications
Binding sitei105 – 1051ShikimateUniRule annotation2 Publications
Binding sitei181 – 1811NADP; via amide nitrogen1 Publication
Binding sitei208 – 2081NADP; via carbonyl oxygenUniRule annotation
Binding sitei210 – 2101ShikimateUniRule annotation2 Publications
Binding sitei230 – 2301NADP; via carbonyl oxygenUniRule annotation1 Publication
Binding sitei237 – 2371ShikimateUniRule annotation3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi125 – 1295NADPUniRule annotation1 Publication

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. shikimate 3-dehydrogenase (NADP+) activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. aromatic amino acid family biosynthetic process Source: UniProtKB-HAMAP
  2. chorismate biosynthetic process Source: UniProtKB-UniPathway
  3. shikimate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciHPY:HP1249-MONOMER.
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:HP_1249
OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifieri85962 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
ProteomesiUP000000429 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263Shikimate dehydrogenase (NADP(+))PRO_0000136007Add
BLAST

Proteomic databases

PRIDEiP56119.

Interactioni

Subunit structurei

Homodimer.UniRule annotation2 Publications

Protein-protein interaction databases

IntActiP56119. 1 interaction.
STRINGi85962.HP1249.

Structurei

Secondary structure

1
263
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1210Combined sources
Helixi18 – 3316Combined sources
Beta strandi34 – 4310Combined sources
Beta strandi46 – 483Combined sources
Helixi50 – 567Combined sources
Beta strandi59 – 646Combined sources
Helixi69 – 757Combined sources
Beta strandi76 – 794Combined sources
Helixi81 – 855Combined sources
Beta strandi91 – 955Combined sources
Beta strandi98 – 1025Combined sources
Helixi105 – 1128Combined sources
Beta strandi120 – 1245Combined sources
Helixi128 – 13912Combined sources
Beta strandi143 – 1475Combined sources
Beta strandi149 – 1513Combined sources
Helixi154 – 1607Combined sources
Beta strandi163 – 1675Combined sources
Beta strandi174 – 1785Combined sources
Helixi183 – 1853Combined sources
Helixi192 – 20110Combined sources
Beta strandi203 – 2086Combined sources
Helixi215 – 2228Combined sources
Helixi231 – 24515Combined sources
Turni246 – 2483Combined sources
Helixi252 – 26211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PHGX-ray1.57A/B1-263[»]
3PHHX-ray1.42A1-263[»]
3PHIX-ray2.04A/B1-263[»]
3PHJX-ray2.30A/B1-263[»]
4FOOX-ray2.55A/B1-263[»]
4FOSX-ray1.72A1-263[»]
4FPXX-ray2.40A/B1-263[»]
4FQ8X-ray2.07A/B1-263[»]
4FR5X-ray2.20A/B1-263[»]
4FSHX-ray2.85A/B1-263[»]
ProteinModelPortaliP56119.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni16 – 183Shikimate bindingUniRule annotation3 Publications

Sequence similaritiesi

Belongs to the shikimate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0169.
KOiK00014.
OMAiSASQIPY.
OrthoDBiEOG64R67G.

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_quinate_DH.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF01488. Shikimate_DH. 1 hit.
PF08501. Shikimate_dh_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00507. aroE. 1 hit.

Sequencei

Sequence statusi: Complete.

P56119-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLKSFGVFG NPIKHSKSPL IHNACFLTFQ KELRFLGHYH PILLPLESHI
60 70 80 90 100
KSEFLHLGLS GANVTLPFKE RAFQVCDKIK GIALECGAVN TLVLENDELV
110 120 130 140 150
GYNTDALGFY LSLKQKNYQN ALILGAGGSA KALACELKKQ GLQVSVLNRS
160 170 180 190 200
SRGLDFFQRL GCDCFMEPPK SAFDLIINAT SASLHNELPL NKEVLKGYFK
210 220 230 240 250
EGKLAYDLAY GFLTPFLSLA KELKTPFQDG KDMLIYQAAL SFEKFSASQI
260
PYSKAFEVMR SVF
Length:263
Mass (Da):29,273
Last modified:November 1, 1997 - v1
Checksum:iA34E5BD3E54C4937
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD08294.1.
PIRiA64676.
RefSeqiNP_208041.1. NC_000915.1.
YP_006935169.1. NC_018939.1.

Genome annotation databases

EnsemblBacteriaiAAD08294; AAD08294; HP_1249.
GeneIDi13870456.
898819.
KEGGiheo:C694_06455.
hpy:HP1249.
PATRICi20593875. VBIHelPyl33062_1308.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD08294.1.
PIRiA64676.
RefSeqiNP_208041.1. NC_000915.1.
YP_006935169.1. NC_018939.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PHGX-ray1.57A/B1-263[»]
3PHHX-ray1.42A1-263[»]
3PHIX-ray2.04A/B1-263[»]
3PHJX-ray2.30A/B1-263[»]
4FOOX-ray2.55A/B1-263[»]
4FOSX-ray1.72A1-263[»]
4FPXX-ray2.40A/B1-263[»]
4FQ8X-ray2.07A/B1-263[»]
4FR5X-ray2.20A/B1-263[»]
4FSHX-ray2.85A/B1-263[»]
ProteinModelPortaliP56119.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP56119. 1 interaction.
STRINGi85962.HP1249.

Proteomic databases

PRIDEiP56119.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD08294; AAD08294; HP_1249.
GeneIDi13870456.
898819.
KEGGiheo:C694_06455.
hpy:HP1249.
PATRICi20593875. VBIHelPyl33062_1308.

Phylogenomic databases

eggNOGiCOG0169.
KOiK00014.
OMAiSASQIPY.
OrthoDBiEOG64R67G.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00087.
BioCyciHPY:HP1249-MONOMER.

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_quinate_DH.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF01488. Shikimate_DH. 1 hit.
PF08501. Shikimate_dh_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00507. aroE. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700392 / 26695.
  2. "Crystal structure of the shikimate 5-dehydrogenase (aroE) from Helicobacter pylori in complex with shikimate and NADPH."
    Cheng W.C., Lin S.C., Wang W.C.
    Submitted (OCT-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) IN COMPLEX WITH SHIKIMATE AND NADP, SUBUNIT.
  3. "Crystal structure of shikimate dehydrogenase (aroE) mutants from Helicobacter pylori in complex with shikimate."
    Cheng W.C., Lin S.C., Wang W.C.
    Submitted (NOV-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH SHIKIMATE, SUBUNIT.
  4. "Crystal structure of shikimate dehydrogenase (aroE) clinical v2356 from Helicobacter pylori in complex with shikimate."
    Cheng W.C., Chen T.J., Wang W.C.
    Submitted (DEC-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH SHIKIMATE.

Entry informationi

Entry nameiAROE_HELPY
AccessioniPrimary (citable) accession number: P56119
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: March 4, 2015
This is version 101 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. Helicobacter pylori
    Helicobacter pylori (strain 26695): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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.