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UniProtKB - Q6KZI8 (KDGA_PICTO)
Protein
2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolase
Gene
PTO1279
Organism
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
Status
Functioni
Involved in the degradation of glucose via the Entner-Doudoroff pathway. Catalyzes the reversible cleavage of 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxygluconate (KDG) forming pyruvate and glyceraldehyde 3-phosphate or glyceraldehyde, respectively. It is also able to catalyze the reversible cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) and 2-keto-3-deoxygalactonate (KDGal). It is equally active with both D- and L-glyceraldehyde.
1 PublicationCatalytic activityi
Kineticsi
- KM=0.3 mM for KDG (at 60 degrees Celsius and pH 6.2)1 Publication
- KM=2.7 mM for pyruvate (at 60 degrees Celsius and pH 6.2)1 Publication
- KM=4.6 mM for glyceraldehyde (at 60 degrees Celsius and pH 6.2)1 Publication
- KM=8 mM for KDPG (at 60 degrees Celsius and pH 6.2)1 Publication
- Vmax=67 µmol/min/mg enzyme with KDG as D-glyceraldehyde (at 60 degrees Celsius and pH 6.2)1 Publication
- Vmax=59 µmol/min/mg enzyme with KDG as L-glyceraldehyde (at 60 degrees Celsius and pH 6.2)1 Publication
- Vmax=50 µmol/min/mg enzyme with KDG as substrate (at 60 degrees Celsius and pH 6.2)1 Publication
- Vmax=0.63 µmol/min/mg enzyme with KDPG as substrate (at 60 degrees Celsius and pH 6.2)1 Publication
pH dependencei
Optimum pH is 5.5, and 50% of activity is found at pH 4.5 and 7.5.1 Publication
Temperature dependencei
Optimum temperature is 65 degrees Celsius. It shows high thermostability. At 70 degrees Celsius, the enzyme does not lose activity upon incubation for 2 hours. The half-lives of the enzyme at 80 degrees Celsius and 90 degrees Celsius are 20 minutes and 15 minutes, respectively.1 Publication
: 2-dehydro-3-deoxy-D-gluconate degradation Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-gluconate. This subpathway is part of the pathway 2-dehydro-3-deoxy-D-gluconate degradation, which is itself part of Carbohydrate acid metabolism.View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-gluconate, the pathway 2-dehydro-3-deoxy-D-gluconate degradation and in Carbohydrate acid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 123 | Proton shuttleBy similarity | 1 | |
Active sitei | 151 | Schiff-base intermediate with substrateBy similarity | 1 |
GO - Molecular functioni
- 2-dehydro-3-deoxy-6-phosphogalactonate aldolase activity Source: UniProtKB
- 2-dehydro-3-deoxy-D-gluconate aldolase activity Source: UniProtKB-EC
- 2-dehydro-3-deoxy-phosphogluconate aldolase activity Source: UniProtKB
- aldehyde-lyase activity Source: UniProtKB
GO - Biological processi
- glucose catabolic process Source: UniProtKB
Keywordsi
Molecular function | Lyase |
Biological process | Carbohydrate metabolism |
Ligand | Schiff base |
Enzyme and pathway databases
BRENDAi | 4.1.2.51, 7518 |
UniPathwayi | UPA00856;UER00829 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Ordered Locus Names:PTO1279 |
Organismi | Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828) |
Taxonomic identifieri | 263820 [NCBI] |
Taxonomic lineagei | Archaea › Candidatus Thermoplasmatota › Thermoplasmata › Thermoplasmatales › Picrophilaceae › Picrophilus › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000422659 | 1 – 266 | 2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolaseAdd BLAST | 266 |
Proteomic databases
PRIDEi | Q6KZI8 |
Interactioni
Subunit structurei
Homotetramer; dimer of dimers.
1 PublicationProtein-protein interaction databases
STRINGi | 263820.PTO1279 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | Q6KZI8 |
SMRi | Q6KZI8 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 36 – 37 | Substrate bindingBy similarity | 2 | |
Regioni | 123 – 125 | Substrate bindingBy similarity | 3 | |
Regioni | 151 – 153 | Substrate bindingBy similarity | 3 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | arCOG04172, Archaea |
HOGENOMi | CLU_049343_5_1_2 |
OMAi | GMDACVP |
Family and domain databases
Gene3Di | 3.20.20.70, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR002220, DapA-like IPR020625, Schiff_base-form_aldolases_AS |
PANTHERi | PTHR12128, PTHR12128, 1 hit |
Pfami | View protein in Pfam PF00701, DHDPS, 1 hit |
PIRSFi | PIRSF001365, DHDPS, 1 hit |
PRINTSi | PR00146, DHPICSNTHASE |
SMARTi | View protein in SMART SM01130, DHDPS, 1 hit |
PROSITEi | View protein in PROSITE PS00666, DHDPS_2, 1 hit |
i Sequence
Sequence statusi: Complete.
Q6KZI8-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MITPLDAHGN IDYNATNILI KYLEGINVDY LFPMGSTGVF PYFTLKERKD
60 70 80 90 100
FLKFVRENSK KPIMAGVGSS SINEVNELMK FSMDIGIEAA VLMPPYYIKL
110 120 130 140 150
NQEAIYHYYK EILSSNDMDL LIYNIPQFTN KIDPETVKNL KSEFSSVKGV
160 170 180 190 200
KDSSADIRGF MEMLSLSDDD FAVFQGQDDL LFTSLELGAS GGVCGTTNFS
210 220 230 240 250
DGIVRLYHEY KNNREMALKI EKNDVIPLMK KLGKYQFPNA YYEYFYKKNN
260
INGGYRPPMY RVGIEI
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE017261 Genomic DNA Translation: AAT43864.1 |
Genome annotation databases
EnsemblBacteriai | AAT43864; AAT43864; PTO1279 |
KEGGi | pto:PTO1279 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE017261 Genomic DNA Translation: AAT43864.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4UXD | X-ray | 2.50 | A/B/C/D | 1-266 | [»] | |
AlphaFoldDBi | Q6KZI8 | |||||
SMRi | Q6KZI8 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 263820.PTO1279 |
Proteomic databases
PRIDEi | Q6KZI8 |
Genome annotation databases
EnsemblBacteriai | AAT43864; AAT43864; PTO1279 |
KEGGi | pto:PTO1279 |
Phylogenomic databases
eggNOGi | arCOG04172, Archaea |
HOGENOMi | CLU_049343_5_1_2 |
OMAi | GMDACVP |
Enzyme and pathway databases
UniPathwayi | UPA00856;UER00829 |
BRENDAi | 4.1.2.51, 7518 |
Family and domain databases
Gene3Di | 3.20.20.70, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR002220, DapA-like IPR020625, Schiff_base-form_aldolases_AS |
PANTHERi | PTHR12128, PTHR12128, 1 hit |
Pfami | View protein in Pfam PF00701, DHDPS, 1 hit |
PIRSFi | PIRSF001365, DHDPS, 1 hit |
PRINTSi | PR00146, DHPICSNTHASE |
SMARTi | View protein in SMART SM01130, DHDPS, 1 hit |
PROSITEi | View protein in PROSITE PS00666, DHDPS_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | KDGA_PICTO | |
Accessioni | Q6KZI8Primary (citable) accession number: Q6KZI8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 26, 2013 |
Last sequence update: | July 5, 2004 | |
Last modified: | May 25, 2022 | |
This is version 93 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families