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Protein

Quinate/shikimate dehydrogenase

Gene

ydiB

Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

The actual biological function of YdiB remains unclear, nor is it known whether 3-dehydroshikimate or quinate represents the natural substrate. Catalyzes the reversible NAD-dependent reduction of both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate (SA) and quinate, respectively. It can use both NAD or NADP for catalysis, however it has higher catalytic efficiency with NAD.UniRule annotation

Catalytic activityi

L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H.UniRule annotation
Shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H.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. Phospho-2-dehydro-3-deoxyheptonate aldolase (aroG), Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-sensitive (aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase (aroF), Phospho-2-dehydro-3-deoxyheptonate aldolase (c1220)
  2. 3-dehydroquinate synthase (aroB)
  3. 3-dehydroquinate dehydratase (aroD)
  4. Quinate/shikimate dehydrogenase (ydiB), Shikimate dehydrogenase (NADP(+)) (aroE)
  5. Shikimate kinase 2 (aroL), Shikimate kinase 1 (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)DescriptionActionsGraphical viewLength
Binding sitei71SubstrateUniRule annotation1
Binding sitei107SubstrateUniRule annotation1
Binding sitei205NAD; via amide nitrogenUniRule annotation1
Binding sitei255NAD; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi132 – 135NADUniRule annotation4
Nucleotide bindingi155 – 158NADUniRule annotation4
Nucleotide bindingi232 – 235NADUniRule annotation4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywordsi

Molecular functionOxidoreductase
Biological processAmino-acid biosynthesis, Aromatic amino acid biosynthesis
LigandNAD, NADP

Enzyme and pathway databases

BioCyciECOL199310:C2087-MONOMER.
UniPathwayiUPA00053; UER00087.

Names & Taxonomyi

Protein namesi
Recommended name:
Quinate/shikimate dehydrogenaseUniRule annotation (EC:1.1.1.282UniRule annotation)
Alternative name(s):
NAD-dependent shikimate 5-dehydrogenaseUniRule annotation
Gene namesi
Name:ydiBUniRule annotation
Ordered Locus Names:c2087
OrganismiEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Taxonomic identifieri199310 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000001410 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001360711 – 288Quinate/shikimate dehydrogenaseAdd BLAST288

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

MINTiMINT-1283296.
STRINGi199310.c2087.

Structurei

3D structure databases

ProteinModelPortaliP0A6D6.
SMRiP0A6D6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the shikimate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105E2X. Bacteria.
COG0169. LUCA.
HOGENOMiHOG000237875.
KOiK05887.
OMAiPFIHNSA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00222. Shikimate_DH_AroE. 1 hit.
MF_01578. Shikimate_DH_YdiB. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR022872. Quinate/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.

Sequencei

Sequence statusi: Complete.

P0A6D6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVTAKYELI GLMAYPIRHS LSPEMQNKAL EKAGLPFTYM AFEVDNDSFP
60 70 80 90 100
GAIEGLKALK MRGTGVSMPN KQLACEYVDE LTPAAKLVGA INTIVNDDGY
110 120 130 140 150
LRGYNTDGTG HIRAIKESGF DIKGKTMVLL GAGGASTAIG AQGAIEGLKE
160 170 180 190 200
IKLFNRRDEF FDKALAFAQR VNENTDCVVT VTDLADQQAF AEALASADIL
210 220 230 240 250
TNGTKVGMKP LENESLVNDI SLLHPGLLVT ECVYNPHMTK LLQQAQQAGC
260 270 280
KTIDGYGMLL WQGAEQFTLW TGKDFPLEYV KQVMGFGA
Length:288
Mass (Da):31,228
Last modified:June 7, 2005 - v1
Checksum:iC3D1415E03820A5A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014075 Genomic DNA. Translation: AAN80547.1.
RefSeqiWP_000383469.1. NC_004431.1.

Genome annotation databases

EnsemblBacteriaiAAN80547; AAN80547; c2087.
KEGGiecc:c2087.
PATRICi18282073. VBIEscCol75197_1953.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014075 Genomic DNA. Translation: AAN80547.1.
RefSeqiWP_000383469.1. NC_004431.1.

3D structure databases

ProteinModelPortaliP0A6D6.
SMRiP0A6D6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1283296.
STRINGi199310.c2087.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN80547; AAN80547; c2087.
KEGGiecc:c2087.
PATRICi18282073. VBIEscCol75197_1953.

Phylogenomic databases

eggNOGiENOG4105E2X. Bacteria.
COG0169. LUCA.
HOGENOMiHOG000237875.
KOiK05887.
OMAiPFIHNSA.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00087.
BioCyciECOL199310:C2087-MONOMER.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00222. Shikimate_DH_AroE. 1 hit.
MF_01578. Shikimate_DH_YdiB. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR022872. Quinate/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.
ProtoNetiSearch...

Entry informationi

Entry nameiYDIB_ECOL6
AccessioniPrimary (citable) accession number: P0A6D6
Secondary accession number(s): P28244, P77647
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: November 2, 2016
This is version 83 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.