Q46857 (DKGA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	275 AA.
Sequence status	Complete.
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 Reference proteome
Gene Ontology (GO)
Biological_process	L-ascorbic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW methylglyoxal catabolic process Inferred from mutant phenotype PubMed 16077126. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	2,5-didehydrogluconate reductase activity Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred from direct assay PubMed 16077126. Source: EcoCyc
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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 2-275.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U28377 Genomic DNA. Translation: AAA69179.1. Frameshift.
U00096 Genomic DNA. Translation: AAC76048.2.
AP009048 Genomic DNA. Translation: BAE77069.1.

PIR

B65088.

RefSeq

NP_417485.4. NC_000913.2.
YP_491205.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

Q46857.

SMR

Q46857. Positions 2-275.

ModBase

Search...

Protein-protein interaction databases

STRING

511145.b3012.

Proteomic databases

PaxDb

Q46857.

PRIDE

Q46857.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76048; AAC76048; b3012.
BAE77069; BAE77069; BAE77069.

GeneID

12933387.
947495.

KEGG

ecj:Y75_p2939.
eco:b3012.

PATRIC

32121440. VBIEscCol129921_3107.

Organism-specific databases

EchoBASE

EB2835.

EcoGene

EG13015. dkgA.

Phylogenomic databases

eggNOG

COG0656.

HOGENOM

HOG000250272.

KO

K06221.

OMA

THHIQTE.

ProtClustDB

PRK11565.

Enzyme and pathway databases

BioCyc

EcoCyc:MONOMER0-148.
ECOL316407:JW5499-MONOMER.
MetaCyc:MONOMER0-148.

Gene expression databases

Genevestigator

Q46857.

Family and domain databases

Gene3D

3.20.20.100. 1 hit.

InterPro

IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]

PANTHER

PTHR11732. PTHR11732. 1 hit.

Pfam

PF00248. Aldo_ket_red. 1 hit.
[Graphical view]

PIRSF

PIRSF000097. AKR. 1 hit.

PRINTS

PR00069. ALDKETRDTASE.

SUPFAM

SSF51430. Aldo/ket_red. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

EvolutionaryTrace

Q46857.

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:	May 1, 2013
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program