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P0A9Q0 (IDNO_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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:
Gluconate 5-dehydrogenase

EC=1.1.1.69
Alternative name(s):
5-keto-D-gluconate 5-reductase
Gene names
Name:idnO
Ordered Locus Names:c5367
OrganismEscherichia coli O6 [Complete proteome] [HAMAP]
Taxonomic identifier217992 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes a reversible reduction of 5-ketoglutanate to form D-gluconate. Dependent on NADP, almost inactive with NAD By similarity.

Catalytic activity

D-gluconate + NAD(P)+ = 5-dehydro-D-gluconate + NAD(P)H.

Pathway

Carbohydrate acid metabolism; L-idonate degradation.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
   Biological processGluconate utilization
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processD-gluconate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiongluconate 5-dehydrogenase activity

Inferred from electronic annotation. Source: EC

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 254254Gluconate 5-dehydrogenase
PRO_0000054703

Regions

Nucleotide binding13 – 3725NADP By similarity

Sites

Active site1581Proton acceptor By similarity
Binding site1451Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A9Q0 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: C5AA4A044CEC1E6E

FASTA25427,563
        10         20         30         40         50         60 
MNDLFSLAGK NILITGSAQG IGFLLATGLG KYGAQIIIND ITAERAELAV EKLHQEGIQA 

        70         80         90        100        110        120 
VAAPFNVTHK HEIDAAVEHI EKDIGPIDVL VNNAGIQRRH PFTEFPEQEW NDVIAVNQTA 

       130        140        150        160        170        180 
VFLVSQAVTR HMVERKAGKV INICSMQSEL GRDTITPYAA SKGAVKMLTR GMCVELARHN 

       190        200        210        220        230        240 
IQVNGIAPGY FKTEMTKALV EDEAFTAWLC KRTPAARWGD PQELIGAAVF LSSKASDFVN 

       250 
GHLLFVDGGM LVAV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN83789.1.
RefSeqNP_757215.1. NC_004431.1.

3D structure databases

ProteinModelPortalP0A9Q0.
SMRP0A9Q0. Positions 1-253.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000040827; EBESCP00000039176; EBESCG00000039877.
GeneID1037302.
GenomeReviewsGene locus c5367 in contig AE014075_GR.
KEGGecc:c5367.
PATRIC18288379. VBIEscCol75197_5030.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009181.
HOGENOMHBG750976.
OMARYMIKRQ.
PhylomeDBP0A9Q0.
ProtClustDBPRK08085.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00046.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIDNO_ECOL6
AccessionPrimary (citable) accession number: P0A9Q0
Secondary accession number(s): P39345
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families