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C4ZYF4 (YDIB_ECOBW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Quinate/shikimate dehydrogenase

EC=1.1.1.282
Alternative name(s):
NAD-dependent shikimate 5-dehydrogenase 2
Gene names
Name:ydiB
Ordered Locus Names:BWG_1506
OrganismEscherichia coli (strain K12 / MC4100 / BW2952) [Complete proteome] [HAMAP]
Taxonomic identifier595496 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H. HAMAP-Rule MF_01578

Shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H. HAMAP-Rule MF_01578

Pathway

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. HAMAP-Rule MF_01578

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01578

Sequence similarities

Belongs to the shikimate dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 288288Quinate/shikimate dehydrogenase HAMAP-Rule MF_01578
PRO_1000215614

Regions

Nucleotide binding131 – 1355NAD By similarity
Nucleotide binding155 – 1584NAD By similarity
Nucleotide binding255 – 2595NAD By similarity

Sites

Active site711Proton acceptor Potential
Binding site1071Substrate By similarity
Binding site2051NAD; via amide nitrogen By similarity
Binding site2351NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
C4ZYF4 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: C3D1415E03820A5A

FASTA28831,228
        10         20         30         40         50         60 
MDVTAKYELI GLMAYPIRHS LSPEMQNKAL EKAGLPFTYM AFEVDNDSFP GAIEGLKALK 

        70         80         90        100        110        120 
MRGTGVSMPN KQLACEYVDE LTPAAKLVGA INTIVNDDGY LRGYNTDGTG HIRAIKESGF 

       130        140        150        160        170        180 
DIKGKTMVLL GAGGASTAIG AQGAIEGLKE IKLFNRRDEF FDKALAFAQR VNENTDCVVT 

       190        200        210        220        230        240 
VTDLADQQAF AEALASADIL TNGTKVGMKP LENESLVNDI SLLHPGLLVT ECVYNPHMTK 

       250        260        270        280 
LLQQAQQAGC KTIDGYGMLL WQGAEQFTLW TGKDFPLEYV KQVMGFGA 

« Hide

References

[1]"Genomic sequencing reveals regulatory mutations and recombinational events in the widely used MC4100 lineage of Escherichia coli K-12."
Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R., Wang L.
J. Bacteriol. 191:4025-4029(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MC4100 / BW2952.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001396 Genomic DNA. Translation: ACR65393.1.
RefSeqYP_002926703.1. NC_012759.1.

3D structure databases

ProteinModelPortalC4ZYF4.
SMRC4ZYF4. Positions 5-288.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING595496.BWG_1506.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR65393; ACR65393; BWG_1506.
GeneID7955690.
KEGGebw:BWG_1506.
PATRIC18272239. VBIEscCol60876_1652.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0169.
HOGENOMHOG000237875.
KOK05887.
OMAVSFEIWT.
OrthoDBEOG64R67G.
ProtClustDBPRK12749.

Enzyme and pathway databases

BioCycECOL595496:GI18-1556-MONOMER.
UniPathwayUPA00053; UER00087.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00222. Shikimate_DH_AroE.
MF_01578. Shikimate_DH_YdiB.
InterProIPR016040. NAD(P)-bd_dom.
IPR022872. Quinate/Shikimate_DH.
IPR013708. Shikimate_DH-bd_N.
IPR022893. Shikimate_quinate_DH.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamPF01488. Shikimate_DH. 1 hit.
PF08501. Shikimate_dh_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameYDIB_ECOBW
AccessionPrimary (citable) accession number: C4ZYF4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: February 19, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways