Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P37672 (DLGD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 109. 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) [Reference proteome] [HAMAP]
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-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.

Sequence similarities

Belongs to the LDH2/MDH2 oxidoreductase family. DlgD subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Nucleotide binding168 – 1747NAD HAMAP-Rule MF_00820
Nucleotide binding224 – 2252NAD HAMAP-Rule MF_00820
Nucleotide binding304 – 3063NAD HAMAP-Rule 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] [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 277:1453-1462(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.
PIRA65157.
RefSeqNP_418032.1. NC_000913.3.
YP_491859.1. NC_007779.1.

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...
MobiDBSearch...

Protein-protein interaction databases

STRING511145.b3575.

Proteomic databases

PRIDEP37672.

Protocols and materials databases

DNASU948096.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76599; AAC76599; b3575.
BAE77718; BAE77718; BAE77718.
GeneID12933552.
948096.
KEGGecj:Y75_p3600.
eco:b3575.
PATRIC32122626. VBIEscCol129921_3690.

Organism-specific databases

EchoBASEEB2187.
EcoGeneEG12279. dlgD.

Phylogenomic databases

eggNOGCOG2055.
HOGENOMHOG000249660.
KOK08092.
OMAGHEFTTI.
OrthoDBEOG6QK4PJ.
PhylomeDBP37672.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP37672.

Family and domain databases

HAMAPMF_00820. Diketo_gul_reduc.
InterProIPR023689. Diketo_gul_Rdtase.
IPR003767. Malate/L-lactate_DH.
[Graphical view]
PANTHERPTHR11091. PTHR11091. 1 hit.
PfamPF02615. Ldh_2. 1 hit.
[Graphical view]
SUPFAMSSF89733. SSF89733. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP37672.
PROP37672.

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: May 14, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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