Reviewed, UniProtKB/Swiss-Prot P39346 (IDND_ECOLI)

Names and origin

Protein names

Recommended name:
    L-idonate 5-dehydrogenase
    EC=1.1.1.264

Gene names

Name:	idnD
Synonyms:	yjgV
Ordered Locus Names:	b4267, JW4224

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the NADH/NADPH-dependent oxidation of L-idonate to 5-ketogluconate (5KG). Ref.4
Catalytic activity	L-idonate + NAD(P)+ = 5-dehydrogluconate + NAD(P)H.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Pathway	Carbohydrate acid metabolism; L-idonic acid degradation.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
Biological process	Gluconate utilization
Ligand	Metal-binding NADP Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	D-gluconate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-idonate 5-dehydrogenase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
lpdA	P0A9P0	1	EBI-552913,EBI-542856

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 343	343	L-idonate 5-dehydrogenase		PRO_0000160881
Sites
	Metal binding	40	1	Zinc 1; catalytic By similarity
	Metal binding	65	1	Zinc 1; catalytic By similarity
	Metal binding	93	1	Zinc 2 By similarity
	Metal binding	96	1	Zinc 2 By similarity
	Metal binding	99	1	Zinc 2 By similarity
	Metal binding	107	1	Zinc 2 By similarity
	Metal binding	153	1	Zinc 1; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	P39346-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 7A3C6E6C0CED6F09	FASTA	343	37,147
	10 20 30 40 50 60 MQVKTQSCVV AGKKTVAVTE QTIDWNNNGT LVQITRGGIC GSDLHYYQEG KVGNFMIKAP 70 80 90 100 110 120 MVLGHEVIGK VIHSDSSELH EGQTVAINPS KPCGHCKYCI EHNENQCTDM RFFGSAMYFP 130 140 150 160 170 180 HVDGGFTRYK MVETSQCVPY PAKADEKVMA FAEPLAVAIH AAHQAGELQG KRVFISGVGP 190 200 210 220 230 240 IGCLIVSAVK TLGAAEIVCA DVSPRSLSLG KEMGADVLVN PQNDDMDHWK AEKGYFDVSF 250 260 270 280 290 300 EVSGHPSSVN TCLEVTRARG VMVQVGMGGA MAEFPMMTLI GKEISLRGSF RFTSEFNTAV 310 320 330 340 SWLANGVINP LPLLSAEYPF TDLEEALRFA GDKTQAAKVQ LVF

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: 7610040] [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: 9278503] [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: 16738553] [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: 9658018] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U14003 Genomic DNA. Translation: AAA97164.1. U00096 Genomic DNA. Translation: AAC77224.1. AP009048 Genomic DNA. Translation: BAE78264.1.
PIR	S56493.
RefSeq	AP_004763.1. NP_418688.1.
3D structure databases
HSSP	HSSP built from PDB template 1E3J based on UniProtKB O96496.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:10010N.
IntAct	P39346. 5 interactions.
Genome annotation databases
GeneID	944769.
GenomeReviews	Gene locus JW4224 in contig AP009048_GR. Gene locus b4267 in contig U00096_GR.
KEGG	ecj:JW4224. eco:b4267.
Organism-specific databases
EchoBASE	EB2430.
EcoGene	EG12541. idnD.
CMR	Search...
Phylogenomic databases
HOGENOM	P39346.
OMA	P39346. EAACSEP.
Enzyme and pathway databases
BioCyc	EcoCyc:IDONDEHYD-MON. MetaCyc:IDONDEHYD-MON.
Family and domain databases
InterPro	IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR002328. ADH_Zn_CS. [Graphical view]
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
PROSITE	PS00059. ADH_ZINC. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

IDND_ECOLI

Accession

Primary (citable) accession number: P39346
Secondary accession number(s): Q2M642

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)