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P37672 (DLGD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3323322,3-diketo-L-gulonate reductase HAMAP MF_00820
PRO_0000083830

Regions

Nucleotide binding168 – 1747NAD HAMAP MF_00820
Nucleotide binding224 – 2252NAD HAMAP MF_00820
Nucleotide binding304 – 3063NAD HAMAP MF_00820

Sites

Active site441Proton donor Probable

Secondary structure

...................................................... 332
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37672 [UniParc].

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

FASTA33236,573
        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' 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.
PIRA65157.
RefSeqNP_418032.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NXUX-ray1.80A/B1-332[»]
1S20X-ray2.20A/B/C/D/E/F/G/H1-332[»]
ProteinModelPortalP37672.
SMRP37672. Positions 1-332.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000001300; EBESCP00000001300; EBESCG00000001078.
EBESCT00000001301; EBESCP00000001301; EBESCG00000001078.
EBESCT00000017384; EBESCP00000016675; EBESCG00000016440.
GeneID948096.
GenomeReviewsGene locus JW3547 in contig AP009048_GR.
Gene locus b3575 in contig U00096_GR.
KEGGecj:JW3547.
eco:b3575.
PATRIC32122626. VBIEscCol129921_3690.

Organism-specific databases

EchoBASEEB2187.
EcoGeneEG12279. dlgD.

Phylogenomic databases

eggNOGCOG2055.
GeneTreeEBGT00050000009495.
HOGENOMHBG293006.
OMATNALAVM.
PhylomeDBP37672.
ProtClustDBPRK13260.

Enzyme and pathway databases

BioCycEcoCyc:EG12279-MONOMER.
MetaCyc:EG12279-MONOMER.

Gene expression databases

GenevestigatorP37672.

Family and domain databases

HAMAPMF_00820. Diketo_gul_reduc.
[Tree]
InterProIPR023689. Diketo_gul_Rdtase.
IPR003767. Malate/L-lactate_DH.
[Graphical view]
KOK08092.
PANTHERPTHR11091. MDH_LDH. 1 hit.
PfamPF02615. Ldh_2. 1 hit.
[Graphical view]
SUPFAMSSF89733. MDH_LDH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDLGD_ECOLI
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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