[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1093/nar/23.12.2105; PubMed=7610040 [NCBI, ExPASy, EBI, Israel, Japan] Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.; "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."; Nucleic Acids Res. 23:2105-2119(1995).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[4]	FUNCTION. PubMed=9658018 [NCBI, ExPASy, EBI, Israel, Japan] Bausch C., Peekhaus N., Utz C., Blais T., Murray E., Lowary T., Conway T.; "Sequence analysis of the GntII (subsidiary) system for gluconate metabolism reveals a novel pathway for L-idonic acid catabolism in Escherichia coli."; J. Bacteriol. 180:3704-3710(1998).

Comments

FUNCTION: Catalyzes a reversible reduction of 5-ketoglutanate to form D-gluconate. Dependent on NADP, almost inactive with NAD.
CATALYTIC ACTIVITY: D-gluconate + NAD(P)⁺ = 5-dehydro-D-gluconate + NAD(P)H.
PATHWAY: Carbohydrate acid metabolism; L-idonic acid degradation .
SUBCELLULAR LOCATION: Cytoplasm (Probable).
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U14003; AAA97163.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC77223.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE78263.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S56492; S56492.

RefSeq

AP_004762.1; -.
NP_418687.1; -.

3D structure databases

HSSP

P25529; 1AHH. [HSSP ENTRY / PDB]

ModBase

P0A9P9.

Enzyme and pathway databases

BioCyc

EcoCyc:GLUCONREDUCT-MON; -.
MetaCyc:GLUCONREDUCT-MON; -.

Organism-specific databases

EchoBASE

EB2429; -.

EcoGene

EG12540; idnO.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0008874;	Molecular function: gluconate 5-dehydrogenase activity (inferred from electronic annotation from EC).
GO:0019521;	Biological process: D-gluconate metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR19410; ADH_short_C2; 1.

Pfam

PF00106; adh_short; 1.
Pfam graphical view of domain structure.

PRINTS

PR00081; GDHRDH.
PR00080; SDRFAMILY.

PROSITE

PS00061; ADH_SHORT; 1.

Genome annotation databases

GeneID

947109; -.

GenomeReviews

AP009048_GR; JW4223.
U00096_GR; b4266.

KEGG

ecj:JW4223; -.
eco:b4266; -.

Phylogenomic databases

HOGENOM

P0A9P9; -.

Genome annotation databases

CMR

P0A9P9; b4266.

Other

ProtoNet

P0A9P9.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Gluconate utilization; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 254`	`254`	`Gluconate 5-dehydrogenase.`	`PRO_0000054702`
`NP_BIND`	`13 37`	`25`	`NADP (By similarity).`
`ACT_SITE`	`158 158`		`Proton acceptor (By similarity).`
`BINDING`	`145 145`		`Substrate (By similarity).`

Sequence information

Length: 254 AA [This is the length of the unprocessed precursor]

Molecular weight: 27563 Da [This is the MW of the unprocessed precursor]

CRC64: C5AA4A044CEC1E6E [This is a checksum on the sequence]

        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

P0A9P9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools