P39346 (IDND_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
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. Ref.4
Cofactor	Binds 2 zinc ions per subunit By similarity.
Pathway	Carbohydrate acid metabolism; L-idonate 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 Reference proteome
Gene Ontology (GO)
Biological process	D-gluconate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW L-idonate catabolic process Inferred from mutant phenotype Ref.4. Source: EcoCyc
Molecular function	L-idonate 5-dehydrogenase activity Inferred from direct assay Ref.4. Source: EcoCyc nucleotide binding Inferred from electronic annotation. Source: InterPro zinc ion 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 – 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 [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, CATALYTIC ACTIVITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U14003 Genomic DNA. Translation: AAA97164.1. U00096 Genomic DNA. Translation: AAC77224.1. AP009048 Genomic DNA. Translation: BAE78264.1.
PIR	S56493.
RefSeq	NP_418688.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P39346.
SMR	P39346. Positions 4-342.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10010N.
IntAct	P39346. 5 interactions.
MINT	MINT-1242659.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000000256; EBESCP00000000256; EBESCG00000000212. EBESCT00000014356; EBESCP00000013647; EBESCG00000013418.
GeneID	944769.
GenomeReviews	Gene locus JW4224 in contig AP009048_GR. Gene locus b4267 in contig U00096_GR.
KEGG	ecj:JW4224. eco:b4267.
PATRIC	32124107. VBIEscCol129921_4398.
Organism-specific databases
EchoBASE	EB2430.
EcoGene	EG12541. idnD.
Phylogenomic databases
eggNOG	COG1063.
GeneTree	EBGT00050000008795.
HOGENOM	HBG753318.
OMA	MGASRTI.
PhylomeDB	P39346.
ProtClustDB	PRK09880.
Enzyme and pathway databases
BioCyc	EcoCyc:IDONDEHYD-MONOMER. MetaCyc:IDONDEHYD-MONOMER.
Gene expression databases
Genevestigator	P39346.
Family and domain databases
InterPro	IPR013149. ADH_C. IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn-type. IPR011032. GroES-like. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00098.
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
SUPFAM	SSF50129. GroES_like. 1 hit.
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:	January 25, 2012
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program