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P50199 (GNO_GLUOX) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:gno
Ordered Locus Names:GOX2187
OrganismGluconobacter oxydans (strain 621H) (Gluconobacter suboxydans) [Complete proteome] [HAMAP]
Taxonomic identifier290633 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconobacter

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the non-phosphorylative, ketogenic oxidation of glucose and oxidizes gluconate to 5-ketogluconate. Dependent on NADP, almost inactive with NAD.

Catalytic activity

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

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   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 – 256256Gluconate 5-dehydrogenase
PRO_0000054701

Regions

Nucleotide binding15 – 3925NADP By similarity

Sites

Active site1601Proton acceptor By similarity
Binding site1471Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P50199 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 38B03C0399C0A07A

FASTA25627,256
        10         20         30         40         50         60 
MSHPDLFSLS GARALVTGAS RGIGLTLAKG LARYGAEVVL NGRNAESLDS AQSGFEAEGL 

        70         80         90        100        110        120 
KASTAVFDVT DQDAVIDGVA AIERDMGPID ILINNAGIQR RAPLEEFSRK DWDDLMSTNV 

       130        140        150        160        170        180 
NAVFFVGQAV ARHMIPRGRG KIVNICSVQS ELARPGIAPY TATKGAVKNL TKGMATDWGR 

       190        200        210        220        230        240 
HGLQINGLAP GYFATEMTER LVADEEFTDW LCKRTPAGRW GQVEELVGAA VFLSSRASSF 

       250 
VNGQVLMVDG GITVSL 

« Hide

References

« Hide 'large scale' references
[1]"Biochemical characterization and sequence analysis of the gluconate:NADP 5-oxidoreductase gene from Gluconobacter oxydans."
Klasen R., Bringer-Meyer S., Sahm H.
J. Bacteriol. 177:2637-2643(1995) [PubMed: 7751271] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-19, CHARACTERIZATION.
Strain: ATCC 19357 / DSM 3503 / JCM 7642 / NBRC 14819 / LMG 1408 / NCIMB 9013.
[2]"Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans."
Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U.
Nat. Biotechnol. 23:195-200(2005) [PubMed: 15665824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 621H.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X80019 Genomic DNA. Translation: CAA56322.1.
CP000009 Genomic DNA. Translation: AAW61923.1.
PIRA57149.
RefSeqYP_192579.1. NC_006677.1.

3D structure databases

ProteinModelPortalP50199.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3250506.
GenomeReviewsGene locus GOX2187 in contig CP000009_GR.
KEGGgox:GOX2187.
NMPDRfig|290633.1.peg.2124.
PATRIC32612322. VBIGluOxy81109_2497.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG750976.
OMAPLEEFEV.

Enzyme and pathway databases

BioCycGOXY290633:GOX2187-MONOMER.

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 nameGNO_GLUOX
AccessionPrimary (citable) accession number: P50199
Secondary accession number(s): Q5FNX3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 25, 2012
This is version 72 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