P37672 (DLGD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2,3-diketo-L-gulonate reductase
Short name=2,3-DKG reductase
EC=1.1.1.130

Alternative name(s):
3-dehydro-L-gulonate 2-dehydrogenase

Gene names

Name:	dlgD
Synonyms:	yiaK
Ordered Locus Names:	b3575, JW3547

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reduction of 2,3-diketo-L-gulonate in the presence of NADH, to form 3-keto-L-gulonate. Ref.5
Catalytic activity	3-dehydro-L-gulonate + NAD(P)+ = (4R,5S)-4,5,6-trihydroxy-2,3-dioxohexanoate + NAD(P)H. HAMAP MF_00820
Enzyme regulation	The enzyme is inhibited by tartrate and D-malate. HAMAP MF_00820
Subunit structure	Homodimer. Ref.6
Subcellular location	Cytoplasm Potential HAMAP MF_00820.
Miscellaneous	NAD is bound in an unusual conformation, at the interface of a dimer of the enzyme. HAMAP MF_00820
Sequence similarities	Belongs to the LDH2/MDH2 oxidoreductase family. DlgD subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-dehydro-L-gulonate 2-dehydrogenase activity Inferred from electronic annotation. Source: EC NAD+ 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 – 332

332

2,3-diketo-L-gulonate reductase HAMAP MF_00820

PRO_0000083830

Regions

Nucleotide binding

168 – 174

7

NAD HAMAP MF_00820

Nucleotide binding

224 – 225

2

NAD HAMAP MF_00820

Nucleotide binding

304 – 306

3

NAD HAMAP MF_00820

Sites

Active site

44

1

Proton donor Probable

Secondary structure

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332

Helix Strand Turn

Details...

Helix

5 – 18

14

Helix

23 – 38

16

Turn

43 – 45

3

Helix

46 – 48

3

Helix

49 – 57

9

Beta strand

68 – 73

6

Beta strand

76 – 80

5

Helix

86 – 104

19

Beta strand

105 – 114

10

Helix

121 – 129

9

Beta strand

133 – 138

6

Beta strand

149 – 151

3

Beta strand

159 – 163

5

Beta strand

169 – 173

5

Beta strand

175 – 178

4

Helix

180 – 188

9

Beta strand

203 – 206

4

Helix

209 – 215

7

Turn

221 – 223

3

Helix

224 – 241

18

Helix

246 – 252

7

Beta strand

254 – 256

3

Beta strand

258 – 266

9

Turn

269 – 271

3

Helix

274 – 289

16

Beta strand

293 – 295

3

Turn

303 – 305

3

Helix

306 – 317

12

Helix

323 – 331

9

Sequences

	Sequence		Length	Mass (Da)
	P37672 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: A411EB14D5C03DF7	FASTA	332	36,573
	10 20 30 40 50 60 MKVTFEQLKA AFNRVLISRG VDSETADACA EMFARTTESG VYSHGVNRFP RFIQQLENGD 70 80 90 100 110 120 IIPDAQPKRI TSLGAIEQWD AQRSIGNLTA KKMMDRAIEL AADHGIGLVA LRNANHWMRG 130 140 150 160 170 180 GSYGWQAAEK GYIGICWTNS IAVMPPWGAK ECRIGTNPLI VAIPSTPITM VDMSMSMFSY 190 200 210 220 230 240 GMLEVNRLAG RQLPVDGGFD DEGNLTKEPG VIEKNRRILP MGYWKGSGMS IVLDMIATLL 250 260 270 280 290 300 SDGASVAEVT QDNSDEYGIS QIFIAIEVDK LIDGPTRDAK LQRIMDYVTS AERADENQAI 310 320 330 RLPGHEFTTL LAENRRNGIT VDDSVWAKIQ AL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R. Nucleic Acids Res. 22:2576-2586(1994) [PubMed: 8041620] [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]	"A rare 920-kilobase chromosomal inversion mediated by IS1 transposition causes constitutive expression of the yiaK-S operon for carbohydrate utilization in Escherichia coli." Badia J., Ibanez E., Sabate M., Baldoma L., Aguilar J. J. Biol. Chem. 273:8376-8381(1998) [PubMed: 9525947] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
[5]	"Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons." Yew W.S., Gerlt J.A. J. Bacteriol. 184:302-306(2002) [PubMed: 11741871] [Abstract] Cited for: FUNCTION. Strain: K12 / MG1655 / ATCC 47076.
[6]	"A novel NAD-binding protein revealed by the crystal structure of 2,3-diketo-L-gulonate reductase (YiaK)." Forouhar F., Lee I., Benach J., Kulkarni K., Xiao R., Acton T.B., Montelione G.T., Tong L. J. Biol. Chem. 279:13148-13155(2004) [PubMed: 14718529] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH NAD AND TARTRATE, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00039 Genomic DNA. Translation: AAB18552.1.
U00096 Genomic DNA. Translation: AAC76599.1.
AP009048 Genomic DNA. Translation: BAE77718.1.
AJ223475 Genomic DNA. Translation: CAA11398.1.

PIR

A65157.

RefSeq

NP_418032.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NXU	X-ray	1.80	A/B	1-332	[»]
1S20	X-ray	2.20	A/B/C/D/E/F/G/H	1-332	[»]

ProteinModelPortal

P37672.

SMR

P37672. Positions 1-332.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001300; EBESCP00000001300; EBESCG00000001078.
EBESCT00000001301; EBESCP00000001301; EBESCG00000001078.
EBESCT00000017384; EBESCP00000016675; EBESCG00000016440.

GeneID

948096.

GenomeReviews

Gene locus JW3547 in contig AP009048_GR.
Gene locus b3575 in contig U00096_GR.

KEGG

ecj:JW3547.
eco:b3575.

PATRIC

32122626. VBIEscCol129921_3690.

Organism-specific databases

EchoBASE

EB2187.

EcoGene

EG12279. dlgD.

Phylogenomic databases

eggNOG

COG2055.

GeneTree

EBGT00050000009495.

HOGENOM

HBG293006.

OMA

TNALAVM.

PhylomeDB

P37672.

ProtClustDB

PRK13260.

Enzyme and pathway databases

BioCyc

EcoCyc:EG12279-MONOMER.
MetaCyc:EG12279-MONOMER.

Gene expression databases

Genevestigator

P37672.

Family and domain databases

HAMAP

MF_00820. Diketo_gul_reduc.
[Tree]

InterPro

IPR023689. Diketo_gul_Rdtase.
IPR003767. Malate/L-lactate_DH.
[Graphical view]

KO

K08092.

PANTHER

PTHR11091. MDH_LDH. 1 hit.

Pfam

PF02615. Ldh_2. 1 hit.
[Graphical view]

SUPFAM

SSF89733. MDH_LDH. 1 hit.

ProtoNet

Search...

Entry information

Entry name

DLGD_ECOLI

Accession

Primary (citable) accession number: P37672
Secondary accession number(s): P76716, Q2M7N8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program