Reviewed, UniProtKB/Swiss-Prot Q46857 (DKGA_ECOLI)

Names and origin

Protein names

Recommended name:
    2,5-diketo-D-gluconic acid reductase A
      Short name=2,5-DKG reductase A
      Short name=2,5-DKGR A
      Short name=25DKGR-A
    EC=1.1.1.274
Alternative name(s):
    AKR5C

Gene names

Name:	dkgA
Synonyms:	yqhE
Ordered Locus Names:	b3012, JW5499

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	275 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Catalytic activity	2-dehydro-D-gluconate + NADP+ = 2,5-didehydro-D-gluconate + NADPH.
Subunit structure	Monomer.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	2-keto-L-gulonic acid is a key intermediate in the production of L-ascorbic acid (vitamin C).
Sequence similarities	Belongs to the aldo/keto reductase family.
Biophysicochemical properties	pH dependence: Optimum pH is 7.5.

Ontologies

Keywords
Biological process	Ascorbate biosynthesis
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	L-ascorbic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2,5-didehydrogluconate reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 275

275

2,5-diketo-D-gluconic acid reductase A

PRO_0000124599

Regions

Nucleotide binding

187 – 241

55

NADP By similarity

Sites

Active site

51

1

Proton donor By similarity

Binding site

107

1

Substrate By similarity

Secondary structure

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275

Helix Strand Turn

Details...

Beta strand

6 – 8

3

Beta strand

14 – 18

5

Helix

27 – 40

14

Beta strand

44 – 46

3

Helix

49 – 51

3

Helix

54 – 63

10

Helix

68 – 70

3

Beta strand

72 – 77

6

Helix

79 – 81

3

Helix

85 – 96

12

Beta strand

101 – 107

7

Turn

111 – 113

3

Helix

116 – 128

13

Beta strand

131 – 139

9

Helix

142 – 152

11

Beta strand

157 – 162

6

Helix

170 – 178

9

Beta strand

182 – 187

6

Turn

188 – 192

5

Turn

194 – 198

5

Helix

200 – 209

10

Helix

213 – 223

11

Helix

235 – 240

6

Helix

251 – 258

8

Turn

270 – 274

5

Sequences

	Sequence		Length	Mass (Da)
	Q46857-1 [UniParc]. Last modified December 15, 1998. Version 3. Checksum: 0FF6E140411BAD43	FASTA	275	31,110
	10 20 30 40 50 60 MANPTVIKLQ DGNVMPQLGL GVWQASNEEV ITAIQKALEV GYRSIDTAAA YKNEEGVGKA 70 80 90 100 110 120 LKNASVNREE LFITTKLWND DHKRPREALL DSLKKLQLDY IDLYLMHWPV PAIDHYVEAW 130 140 150 160 170 180 KGMIELQKEG LIKSIGVCNF QIHHLQRLID ETGVTPVINQ IELHPLMQQR QLHAWNATHK 190 200 210 220 230 240 IQTESWSPLA QGGKGVFDQK VIRDLADKYG KTPAQIVIRW HLDSGLVVIP KSVTPSRIAE 250 260 270 NFDVWDFRLD KDELGEIAKL DQGKRLGPDP DQFGG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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.
[3]	"Identification of the yqhE and yafB genes encoding two 2,5-diketo-D-gluconate reductases in Escherichia coli." Yum D.-Y., Lee B.-Y., Pan J.-G. Appl. Environ. Microbiol. 65:3341-3346(1999) [PubMed: 10427017] [Abstract] Cited for: CHARACTERIZATION. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Purification and identification of an Escherichia coli beta-keto ester reductase as 2,5-diketo-D-gluconate reductase YqhE." Habrych M., Rodriguez S., Stewart J.D. Biotechnol. Prog. 18:257-261(2002) [PubMed: 11934293] [Abstract] Cited for: CHARACTERIZATION.
[5]	"Crystal structure of Escherichia coli DkgA, a broad-specificity aldo-keto reductase." Jeudy S., Monchois V., Maza C., Claverie J.-M., Abergel C. Proteins 62:302-307(2006) [PubMed: 16284956] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 2-275.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U28377 Genomic DNA. Translation: AAA69179.1. Frameshift.
U00096 Genomic DNA. Translation: AAC76048.1. Different initiation.
AP009048 Genomic DNA. Translation: BAE77069.1.

PIR

B65088.

RefSeq

AP_003563.1.
NP_417485.4.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MZR	X-ray	2.13	A/B	2-275	[»]

ModBase

Search...

Genome annotation databases

GeneID

947495.

GenomeReviews

Gene locus JW5499 in contig AP009048_GR.
Gene locus b3012 in contig U00096_GR.

KEGG

ecj:JW5499.
eco:b3012.

Organism-specific databases

EchoBASE

EB2835.

EcoGene

EG13015. dkgA.

CMR

Search...

Phylogenomic databases

HOGENOM

Q46857.

OMA

Q46857. QIELHPM.

Enzyme and pathway databases

BioCyc

EcoCyc:MON0-148.
MetaCyc:MON0-148.

Family and domain databases

InterPro

IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
[Graphical view]

Gene3D

G3DSA:3.20.20.100. Aldo/ket_red. 1 hit.

PANTHER

PTHR11732. Aldo/ket_red. 1 hit.

Pfam

PF00248. Aldo_ket_red. 1 hit.
[Graphical view]

ProDom

PD000288. Aldo/ket_red. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DKGA_ECOLI

Accession

Primary (citable) accession number: Q46857
Secondary accession number(s): Q2M9I7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	December 15, 1998
Last modified:	June 16, 2009
This is version 67 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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