UniProtKB - P37769 (KDUD_ECOLI)
Protein
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase
Gene
kduD
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the reversible reduction of 2,5-diketo-3-deoxygluconate (DKII or 4,6-dihydroxy-2,5-dioxohexanoate) into 2-keto-3-deoxygluconate (KDG or 2-dehydro-3-deoxygluconate) with a concomitant oxidation of NADH (Ref. 4). To a lesser extent, can also reduce 5-keto-D-gluconate and oxidize D-gluconate and 1,2-propanediol (PubMed:24509771). Together with KduI, seems to play a role in the catabolism of hexuronates under osmotic stress conditions, substituting for the regular hexuronate degrading enzymes UxaABC and UxuAB whose expression is repressed in these conditions (PubMed:23437267). In vitro, also exhibits NADH-dependent 20-ketosteroid reductase activity against eukaryotic steroid hormone 11-deoxycorticosterone (11-DOC), which is converted into the product 4-pregnen-20,21-diol-3-one. In addition to 11-DOC, five other C21 steroid compounds (11-deoxycortisol, cortisol, corticosterone, cortisone, and 21-hydroxypregnenolone) are reduced by KduD, but steroids lacking the hydroxyl group at C21 position, such as pregnenolone, testosterone propionate, cortisone acetate, or progesterone, cannot be used as substrate (PubMed:24509771).3 Publications
Caution
Most strains of E.coli do not exhibit 20-ketosteroid reductase activity against steroid substrates such as 11-DOC, despite containing a full-length kduD gene. This activity is observed in the K12 / DH5-alpha strain, whose disruption of the kdgR gene leads to the constitutive expression of KduD in this strain.1 Publication
Catalytic activityi
- 2-dehydro-3-deoxy-D-gluconate + NAD+ = 3-deoxy-D-glycero-2,5-hexodiulosonate + H+ + NADH1 PublicationEC:1.1.1.1271 Publication
Kineticsi
kcat is 3.1 min(-1) for 11-DOC reduction. kcat is 16.6 min(-1) for 11-deoxycortisol (RSS) reduction. kcat is 58.3 min(-1) for D-gluconate oxidation. kcat is 30.7 min(-1) for 5-keto-D-gluconate reduction. kcat is 18.3 min(-1) for 1,2-propanediol oxidation.1 Publication
- KM=30 mM for 2-keto-3-deoxygluconate1 Publication
- KM=0.230 mM for 11-deoxycorticosterone1 Publication
- KM=0.190 mM for 11-deoxycortisol1 Publication
- KM=544.8 mM for D-gluconate1 Publication
- KM=184.5 mM for 5-keto-D-gluconate1 Publication
- KM=3231 mM for 1,2-propanediol1 Publication
- KM=0.037 mM for NADH1 Publication
- KM=0.285 mM for NAD+1 Publication
pH dependencei
Optimum pH is 7.0 for the reduction of 11-DOC, and 9.5 for the oxidation of D-gluconate.1 Publication
Temperature dependencei
Optimum temperature is 37 degrees Celsius for the reduction of 11-DOC.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 145 | SubstrateBy similarity | 1 | |
Active sitei | 158 | Proton acceptorPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 14 – 38 | NADBy similarityAdd BLAST | 25 |
GO - Molecular functioni
- 11-deoxycorticosterone reductase activity Source: RHEA
- 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase activity Source: UniProtKB-EC
- 2-deoxy-D-gluconate 3-dehydrogenase activity Source: InterPro
- NAD binding Source: InterPro
- oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: EcoCyc
- steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: EcoCyc
GO - Biological processi
- D-galacturonate catabolic process Source: EcoCyc
- D-glucuronate catabolic process Source: EcoCyc
Keywordsi
Molecular function | Oxidoreductase |
Ligand | NAD |
Enzyme and pathway databases
BioCyci | EcoCyc:KDUD-MONOMER MetaCyc:KDUD-MONOMER |
Names & Taxonomyi
Protein namesi | Recommended name: 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase1 Publication (EC:1.1.1.1271 Publication)Alternative name(s): 2-deoxy-D-gluconate 3-dehydrogenase1 Publication 2-keto-3-deoxygluconate 5-dehydrogenase 2-keto-3-deoxygluconate oxidoreductase1 Publication Short name: KDG oxidoreductase 20-ketosteroid reductase1 Publication (EC:1.1.1.-1 Publication) |
Gene namesi | Name:kduD1 Publication Synonyms:ygeC, yqeD Ordered Locus Names:b2842, JW2810 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Biotechnological usei
Could be used for the production of valuable bioactive 20-hydroxysteroids; these compounds have potential for pharmaceutical applications as inhibitors of steroid hormone metabolizing enzymes, for the treatment of breast cancer, endometriosis, and prostate diseases in humans.1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000054715 | 1 – 253 | 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenaseAdd BLAST | 253 |
Proteomic databases
jPOSTi | P37769 |
PaxDbi | P37769 |
PRIDEi | P37769 |
Expressioni
Inductioni
Is under the control of KdgR repressor (Probable). Its expression is up-regulated in the presence of galacturonate and glucuronate (PubMed:23437267). Is also up-regulated in intestinal E.coli of mice fed a lactose-rich diet and down-regulated in E.coli of mice on a casein-rich diet (PubMed:22427493).1 Publication2 Publications
Interactioni
Subunit structurei
Homotetramer.
1 PublicationProtein-protein interaction databases
BioGRIDi | 4262312, 35 interactors |
IntActi | P37769, 2 interactors |
STRINGi | 511145.b2842 |
Family & Domainsi
Sequence similaritiesi
Belongs to the short-chain dehydrogenases/reductases (SDR) family.Curated
Phylogenomic databases
eggNOGi | COG1028, Bacteria |
HOGENOMi | CLU_010194_1_1_6 |
InParanoidi | P37769 |
PhylomeDBi | P37769 |
Family and domain databases
InterProi | View protein in InterPro IPR011286, 2-deoxy-D-gluc_3_DH IPR036291, NAD(P)-bd_dom_sf IPR020904, Sc_DH/Rdtase_CS IPR002347, SDR_fam |
PRINTSi | PR00081, GDHRDH PR00080, SDRFAMILY |
SUPFAMi | SSF51735, SSF51735, 1 hit |
TIGRFAMsi | TIGR01832, kduD, 1 hit |
PROSITEi | View protein in PROSITE PS00061, ADH_SHORT, 1 hit |
i Sequence
Sequence statusi: Complete.
P37769-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MILSAFSLEG KVAVVTGCDT GLGQGMALGL AQAGCDIVGI NIVEPTETIE
60 70 80 90 100
QVTALGRRFL SLTADLRKID GIPALLDRAV AEFGHIDILV NNAGLIRRED
110 120 130 140 150
ALEFSEKDWD DVMNLNIKSV FFMSQAAAKH FIAQGNGGKI INIASMLSFQ
160 170 180 190 200
GGIRVPSYTA SKSGVMGVTR LMANEWAKHN INVNAIAPGY MATNNTQQLR
210 220 230 240 250
ADEQRSAEIL DRIPAGRWGL PSDLMGPIVF LASSASDYVN GYTIAVDGGW
LAR
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U29581 Genomic DNA Translation: AAB40489.1 U00096 Genomic DNA Translation: AAC75881.1 AP009048 Genomic DNA Translation: BAE76911.1 J03732 Genomic DNA No translation available. |
PIRi | C65067 |
RefSeqi | NP_417319.1, NC_000913.3 WP_000603502.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC75881; AAC75881; b2842 BAE76911; BAE76911; BAE76911 |
GeneIDi | 57730356 947323 |
KEGGi | ecj:JW2810 eco:b2842 |
PATRICi | fig|1411691.4.peg.3892 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U29581 Genomic DNA Translation: AAB40489.1 U00096 Genomic DNA Translation: AAC75881.1 AP009048 Genomic DNA Translation: BAE76911.1 J03732 Genomic DNA No translation available. |
PIRi | C65067 |
RefSeqi | NP_417319.1, NC_000913.3 WP_000603502.1, NZ_LN832404.1 |
3D structure databases
SMRi | P37769 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 4262312, 35 interactors |
IntActi | P37769, 2 interactors |
STRINGi | 511145.b2842 |
Proteomic databases
jPOSTi | P37769 |
PaxDbi | P37769 |
PRIDEi | P37769 |
Genome annotation databases
EnsemblBacteriai | AAC75881; AAC75881; b2842 BAE76911; BAE76911; BAE76911 |
GeneIDi | 57730356 947323 |
KEGGi | ecj:JW2810 eco:b2842 |
PATRICi | fig|1411691.4.peg.3892 |
Organism-specific databases
EchoBASEi | EB2264 |
Phylogenomic databases
eggNOGi | COG1028, Bacteria |
HOGENOMi | CLU_010194_1_1_6 |
InParanoidi | P37769 |
PhylomeDBi | P37769 |
Enzyme and pathway databases
BioCyci | EcoCyc:KDUD-MONOMER MetaCyc:KDUD-MONOMER |
Miscellaneous databases
PROi | PR:P37769 |
Family and domain databases
InterProi | View protein in InterPro IPR011286, 2-deoxy-D-gluc_3_DH IPR036291, NAD(P)-bd_dom_sf IPR020904, Sc_DH/Rdtase_CS IPR002347, SDR_fam |
PRINTSi | PR00081, GDHRDH PR00080, SDRFAMILY |
SUPFAMi | SSF51735, SSF51735, 1 hit |
TIGRFAMsi | TIGR01832, kduD, 1 hit |
PROSITEi | View protein in PROSITE PS00061, ADH_SHORT, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | KDUD_ECOLI | |
Accessioni | P37769Primary (citable) accession number: P37769 Secondary accession number(s): Q2M9Z5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1994 |
Last sequence update: | October 1, 1996 | |
Last modified: | April 7, 2021 | |
This is version 150 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families