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Protein

2,3-diketo-L-gulonate reductase

Gene

dlgD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of 2,3-diketo-L-gulonate in the presence of NADH, to form 3-keto-L-gulonate.1 Publication

Catalytic activityi

3-dehydro-L-gulonate + NAD(P)+ = (4R,5S)-4,5,6-trihydroxy-2,3-dioxohexanoate + NAD(P)H.

Enzyme regulationi

The enzyme is inhibited by tartrate and D-malate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei44Proton donorCurated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi168 – 174NAD7
Nucleotide bindingi224 – 225NAD2
Nucleotide bindingi304 – 306NAD3

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
2,3-diketo-L-gulonate reductase (EC:1.1.1.130)
Short name:
2,3-DKG reductase
Alternative name(s):
3-dehydro-L-gulonate 2-dehydrogenase
Gene namesi
Name:dlgD
Synonyms:yiaK
Ordered Locus Names:b3575, JW3547
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12279. dlgD.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000838301 – 3322,3-diketo-L-gulonate reductaseAdd BLAST332

Proteomic databases

PaxDbiP37672.
PRIDEiP37672.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4262546. 12 interactors.
STRINGi511145.b3575.

Structurei

Secondary structure

1332
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 18Combined sources14
Helixi23 – 38Combined sources16
Turni43 – 45Combined sources3
Helixi46 – 48Combined sources3
Helixi49 – 57Combined sources9
Beta strandi68 – 73Combined sources6
Beta strandi76 – 80Combined sources5
Helixi86 – 104Combined sources19
Beta strandi105 – 114Combined sources10
Helixi121 – 129Combined sources9
Beta strandi133 – 138Combined sources6
Beta strandi149 – 151Combined sources3
Beta strandi159 – 163Combined sources5
Beta strandi169 – 173Combined sources5
Beta strandi175 – 178Combined sources4
Helixi180 – 188Combined sources9
Beta strandi203 – 206Combined sources4
Helixi209 – 215Combined sources7
Turni221 – 223Combined sources3
Helixi224 – 241Combined sources18
Helixi246 – 252Combined sources7
Beta strandi254 – 256Combined sources3
Beta strandi258 – 266Combined sources9
Turni269 – 271Combined sources3
Helixi274 – 289Combined sources16
Beta strandi293 – 295Combined sources3
Turni303 – 305Combined sources3
Helixi306 – 317Combined sources12
Helixi323 – 331Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NXUX-ray1.80A/B1-332[»]
1S20X-ray2.20A/B/C/D/E/F/G/H1-332[»]
ProteinModelPortaliP37672.
SMRiP37672.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37672.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105DG4. Bacteria.
COG2055. LUCA.
HOGENOMiHOG000249660.
KOiK08092.
OMAiAIKNTNH.
PhylomeDBiP37672.

Family and domain databases

HAMAPiMF_00820. Diketo_gul_reduc. 1 hit.
InterProiIPR023689. Diketo_gul_Rdtase.
IPR003767. Malate/L-lactate_DH.
[Graphical view]
PANTHERiPTHR11091. PTHR11091. 1 hit.
PfamiPF02615. Ldh_2. 1 hit.
[Graphical view]
SUPFAMiSSF89733. SSF89733. 1 hit.

Sequencei

Sequence statusi: Complete.

P37672-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVTFEQLKA AFNRVLISRG VDSETADACA EMFARTTESG VYSHGVNRFP
60 70 80 90 100
RFIQQLENGD IIPDAQPKRI TSLGAIEQWD AQRSIGNLTA KKMMDRAIEL
110 120 130 140 150
AADHGIGLVA LRNANHWMRG GSYGWQAAEK GYIGICWTNS IAVMPPWGAK
160 170 180 190 200
ECRIGTNPLI VAIPSTPITM VDMSMSMFSY GMLEVNRLAG RQLPVDGGFD
210 220 230 240 250
DEGNLTKEPG VIEKNRRILP MGYWKGSGMS IVLDMIATLL SDGASVAEVT
260 270 280 290 300
QDNSDEYGIS QIFIAIEVDK LIDGPTRDAK LQRIMDYVTS AERADENQAI
310 320 330
RLPGHEFTTL LAENRRNGIT VDDSVWAKIQ AL
Length:332
Mass (Da):36,573
Last modified:November 1, 1997 - v2
Checksum:iA411EB14D5C03DF7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18552.1.
U00096 Genomic DNA. Translation: AAC76599.1.
AP009048 Genomic DNA. Translation: BAE77718.1.
AJ223475 Genomic DNA. Translation: CAA11398.1.
PIRiA65157.
RefSeqiNP_418032.1. NC_000913.3.
WP_000869037.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76599; AAC76599; b3575.
BAE77718; BAE77718; BAE77718.
GeneIDi948096.
KEGGiecj:JW3547.
eco:b3575.
PATRICi32122626. VBIEscCol129921_3690.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18552.1.
U00096 Genomic DNA. Translation: AAC76599.1.
AP009048 Genomic DNA. Translation: BAE77718.1.
AJ223475 Genomic DNA. Translation: CAA11398.1.
PIRiA65157.
RefSeqiNP_418032.1. NC_000913.3.
WP_000869037.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NXUX-ray1.80A/B1-332[»]
1S20X-ray2.20A/B/C/D/E/F/G/H1-332[»]
ProteinModelPortaliP37672.
SMRiP37672.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262546. 12 interactors.
STRINGi511145.b3575.

Proteomic databases

PaxDbiP37672.
PRIDEiP37672.

Protocols and materials databases

DNASUi948096.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76599; AAC76599; b3575.
BAE77718; BAE77718; BAE77718.
GeneIDi948096.
KEGGiecj:JW3547.
eco:b3575.
PATRICi32122626. VBIEscCol129921_3690.

Organism-specific databases

EchoBASEiEB2187.
EcoGeneiEG12279. dlgD.

Phylogenomic databases

eggNOGiENOG4105DG4. Bacteria.
COG2055. LUCA.
HOGENOMiHOG000249660.
KOiK08092.
OMAiAIKNTNH.
PhylomeDBiP37672.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP37672.
PROiP37672.

Family and domain databases

HAMAPiMF_00820. Diketo_gul_reduc. 1 hit.
InterProiIPR023689. Diketo_gul_Rdtase.
IPR003767. Malate/L-lactate_DH.
[Graphical view]
PANTHERiPTHR11091. PTHR11091. 1 hit.
PfamiPF02615. Ldh_2. 1 hit.
[Graphical view]
SUPFAMiSSF89733. SSF89733. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDLGD_ECOLI
AccessioniPrimary (citable) accession number: P37672
Secondary accession number(s): P76716, Q2M7N8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

NAD is bound in an unusual conformation, at the interface of a dimer of the enzyme.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.