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Protein

Shikimate dehydrogenase (NADP(+))

Gene

aroE

Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
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: 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 (aroD)
  4. Shikimate dehydrogenase (NADP(+)) (aroE), Shikimate dehydrogenase (NADP(+)) (aroE), 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 sitei73 – 731ShikimateUniRule annotation1 Publication
Active sitei77 – 771Proton acceptorUniRule annotation1 Publication
Binding sitei98 – 981ShikimateUniRule annotation1 Publication
Binding sitei113 – 1131ShikimateUniRule annotation1 Publication
Binding sitei214 – 2141NADP1 Publication
Binding sitei238 – 2381NADP; via carbonyl oxygenUniRule annotation1 Publication
Binding sitei240 – 2401ShikimateUniRule annotation
Binding sitei261 – 2611NADP; via carbonyl oxygenUniRule annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi137 – 1415NADPUniRule annotation1 Publication
Nucleotide bindingi161 – 1644NAD1 Publication

GO - Molecular functioni

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

BioCyciLMON169963:LMO0490-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:lmo0490
OrganismiListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Taxonomic identifieri169963 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
Proteomesi
  • UP000000817 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 291291Shikimate dehydrogenase (NADP(+))PRO_0000136014Add
BLAST

Proteomic databases

PaxDbiQ8Y9N5.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi169963.lmo0490.

Structurei

Secondary structure

1
291
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 229Combined sources
Helixi28 – 3912Combined sources
Beta strandi43 – 497Combined sources
Helixi52 – 6413Combined sources
Beta strandi69 – 724Combined sources
Turni77 – 793Combined sources
Helixi80 – 834Combined sources
Beta strandi85 – 873Combined sources
Helixi89 – 946Combined sources
Beta strandi98 – 1036Combined sources
Beta strandi106 – 1105Combined sources
Helixi113 – 12311Combined sources
Beta strandi131 – 1366Combined sources
Helixi140 – 15112Combined sources
Beta strandi155 – 1617Combined sources
Helixi167 – 18014Combined sources
Beta strandi184 – 1896Combined sources
Helixi193 – 2019Combined sources
Beta strandi204 – 2085Combined sources
Helixi226 – 2283Combined sources
Beta strandi234 – 2385Combined sources
Beta strandi241 – 2444Combined sources
Helixi246 – 2538Combined sources
Beta strandi257 – 2593Combined sources
Helixi262 – 27716Combined sources
Helixi283 – 2908Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TNLX-ray1.45A/B/C/D1-291[»]
3TOZX-ray2.20A/B/C/D/E/F/G/H1-291[»]
ProteinModelPortaliQ8Y9N5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 283Shikimate bindingUniRule annotation1 Publication

Sequence similaritiesi

Belongs to the shikimate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105E2X. Bacteria.
COG0169. LUCA.
HOGENOMiHOG000237875.
KOiK00014.
OMAiSIFARND.
OrthoDBiEOG64R67G.
PhylomeDBiQ8Y9N5.

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.
[Graphical view]
PfamiPF08501. Shikimate_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00507. aroE. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8Y9N5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNKITERIT GHTELIGLIA TPIRHSLSPT MHNEAFAKLG LDYVYLAFEV
60 70 80 90 100
GDKELKDVVQ GFRAMNLRGW NVSMPNKTNI HKYLDKLSPA AELVGAVNTV
110 120 130 140 150
VNDDGVLTGH ITDGTGYMRA LKEAGHDIIG KKMTICGAGG AATAICIQAA
160 170 180 190 200
LDGVKEISIF NRKDDFYANA EKTVEKINSK TDCKAQLFDI EDHEQLRKEI
210 220 230 240 250
AESVIFTNAT GVGMKPFEGE TLLPSADMLR PELIVSDVVY KPTKTRLLEI
260 270 280 290
AEEQGCQTLN GLGMMLWQGA KAFEIWTHKE MPVDYIKEIL F
Length:291
Mass (Da):32,161
Last modified:March 1, 2002 - v1
Checksum:iBDBDFF2732CD7D5D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591975 Genomic DNA. Translation: CAC98569.1.
PIRiAC1136.
RefSeqiNP_464018.1. NC_003210.1.
WP_003725703.1. NC_003210.1.

Genome annotation databases

EnsemblBacteriaiCAC98569; CAC98569; CAC98569.
GeneIDi985396.
KEGGilmo:lmo0490.
PATRICi20310047. VBILisMon69206_0509.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591975 Genomic DNA. Translation: CAC98569.1.
PIRiAC1136.
RefSeqiNP_464018.1. NC_003210.1.
WP_003725703.1. NC_003210.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TNLX-ray1.45A/B/C/D1-291[»]
3TOZX-ray2.20A/B/C/D/E/F/G/H1-291[»]
ProteinModelPortaliQ8Y9N5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi169963.lmo0490.

Proteomic databases

PaxDbiQ8Y9N5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC98569; CAC98569; CAC98569.
GeneIDi985396.
KEGGilmo:lmo0490.
PATRICi20310047. VBILisMon69206_0509.

Phylogenomic databases

eggNOGiENOG4105E2X. Bacteria.
COG0169. LUCA.
HOGENOMiHOG000237875.
KOiK00014.
OMAiSIFARND.
OrthoDBiEOG64R67G.
PhylomeDBiQ8Y9N5.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00087.
BioCyciLMON169963:LMO0490-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_DH_fam.
[Graphical view]
PfamiPF08501. Shikimate_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00507. aroE. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-679 / EGD-e.
  2. "Crystal structure of shikimate 5-dehydrogenase Listeria monocytogenes in complex with shikimate and NAD."
    Center for Structural Genomics of Infectious Diseases (CSGID)
    Submitted (SEP-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH SHIKIMATE AND NADP, SUBUNIT.

Entry informationi

Entry nameiAROE_LISMO
AccessioniPrimary (citable) accession number: Q8Y9N5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: March 1, 2002
Last modified: February 17, 2016
This is version 100 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.