P0A9P9 (IDNO_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Gluconate 5-dehydrogenase
EC=1.1.1.69

Alternative name(s):
5-keto-D-gluconate 5-reductase

Gene names

Name:	idnO
Synonyms:	yjgU
Ordered Locus Names:	b4266, JW4223

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	254 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes a reversible reduction of 5-ketoglutanate to form D-gluconate. Dependent on NADP, almost inactive with NAD. Ref.4
Catalytic activity	D-gluconate + NAD(P)+ = 5-dehydro-D-gluconate + NAD(P)H.
Pathway	Carbohydrate acid metabolism; L-idonate degradation.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Biological process	Gluconate utilization
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	D-gluconate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW L-idonate catabolic process Inferred from expression pattern Ref.4. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	gluconate 5-dehydrogenase activity Inferred from direct assay PubMed 10427017Ref.4. Source: EcoCyc nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 254	254	Gluconate 5-dehydrogenase		PRO_0000054702
Regions
	Nucleotide binding	13 – 37	25	NADP By similarity
Sites
	Active site	158	1	Proton acceptor By similarity
	Binding site	145	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A9P9 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: C5AA4A044CEC1E6E	FASTA	254	27,563
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Sequence analysis of the GntII (subsidiary) system for gluconate metabolism reveals a novel pathway for L-idonic acid catabolism in Escherichia coli." Bausch C., Peekhaus N., Utz C., Blais T., Murray E., Lowary T., Conway T. J. Bacteriol. 180:3704-3710(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U14003 Genomic DNA. Translation: AAA97163.1. U00096 Genomic DNA. Translation: AAC77223.1. AP009048 Genomic DNA. Translation: BAE78263.1.
PIR	S56492.
RefSeq	NP_418687.1. NC_000913.2. YP_492404.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0A9P9.
SMR	P0A9P9. Positions 3-254.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0A9P9. 5 interactions.
MINT	MINT-1231433.
STRING	511145.b4266.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC77223; AAC77223; b4266. BAE78263; BAE78263; BAE78263.
GeneID	12933736. 947109.
KEGG	ecj:Y75_p4149. eco:b4266.
PATRIC	32124105. VBIEscCol129921_4397.
Organism-specific databases
EchoBASE	EB2429.
EcoGene	EG12540. idnO.
Phylogenomic databases
eggNOG	COG1028.
KO	K00046.
OMA	VNICSMQ.
ProtClustDB	PRK08085.
Enzyme and pathway databases
BioCyc	EcoCyc:GLUCONREDUCT-MONOMER. ECOL316407:JW4223-MONOMER. MetaCyc:GLUCONREDUCT-MONOMER.
UniPathway	UPA00793.
Gene expression databases
Genevestigator	P0A9P9.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR020904. Sc_DH/Rdtase_CS. [Graphical view]
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

IDNO_ECOLI

Accession

Primary (citable) accession number: P0A9P9
Secondary accession number(s): P39345, Q2M643

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program