2,3-diketo-L-gulonate reductase - Escherichia coli (strain K12)

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P37672 (DLGD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 102. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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) [Reference proteome] [HAMAP]

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-Rule MF_00820
Enzyme regulation	The enzyme is inhibited by tartrate and D-malate. HAMAP-Rule MF_00820
Subunit structure	Homodimer. Ref.6
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_00820.
Miscellaneous	NAD is bound in an unusual conformation, at the interface of a dimer of the enzyme. HAMAP-Rule 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: HAMAP NAD+ binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred from direct assay Ref.6. Source: EcoCyc
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-Rule MF_00820

PRO_0000083830

Regions

Nucleotide binding

168 – 174

NAD HAMAP-Rule MF_00820

Nucleotide binding

224 – 225

NAD HAMAP-Rule MF_00820

Nucleotide binding

304 – 306

NAD HAMAP-Rule MF_00820

Sites

Active site

Proton donor Probable

Secondary structure

332

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P37672 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: A411EB14D5C03DF7
Show »

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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
YP_491859.1. NC_007779.1.

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...

Protein-protein interaction databases

STRING

511145.b3575.

Proteomic databases

PRIDE

P37672.

Protocols and materials databases

DNASU

948096.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76599; AAC76599; b3575.
BAE77718; BAE77718; BAE77718.

GeneID

12933552.
948096.

KEGG

ecj:Y75_p3600.
eco:b3575.

PATRIC

32122626. VBIEscCol129921_3690.

Organism-specific databases

EchoBASE

EB2187.

EcoGene

EG12279. dlgD.

Phylogenomic databases

eggNOG

COG2055.

HOGENOM

HOG000249660.

K08092.

OMA

VDERVWA.

ProtClustDB

PRK13260.

Enzyme and pathway databases

BioCyc

EcoCyc:EG12279-MONOMER.
ECOL316407:JW3547-MONOMER.
MetaCyc:EG12279-MONOMER.

Gene expression databases

Genevestigator

P37672.

Family and domain databases

HAMAP

MF_00820. Diketo_gul_reduc.

InterPro

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

PANTHER

PTHR11091. PTHR11091. 1 hit.

Pfam

PF02615. Ldh_2. 1 hit.
[Graphical view]

SUPFAM

SSF89733. MDH_LDH. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P37672.

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:	May 1, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents