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Protein

2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolase

Gene

kdgA

Organism
Thermoproteus tenax
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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 not able to use 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) and 2-keto-3-deoxygalactonate (KDGal) as substrate.3 Publications

Catalytic activityi

2-dehydro-3-deoxy-6-phosphate-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate.2 Publications
2-dehydro-3-deoxy-D-gluconate = pyruvate + D-glyceraldehyde.2 Publications

Pathwayi: 2-dehydro-3-deoxy-D-gluconate degradation

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.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. 2-dehydro-3-deoxygluconokinase (kdgK)
  2. 2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolase (kdgA)
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 keyPosition(s)DescriptionActionsGraphical viewLength
Sitei148Proton shuttle1
Active sitei173Schiff-base intermediate with substrate1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BRENDAi4.1.2.14. 6329.
UniPathwayiUPA00856; UER00829.

Names & Taxonomyi

Protein namesi
Recommended name:
2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolase (EC:4.1.2.142 Publications, EC:4.1.2.512 Publications)
Short name:
KD(P)G aldolase1 Publication
Gene namesi
Name:kdgA
OrganismiThermoproteus tenax
Taxonomic identifieri2271 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaeThermoproteus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004226601 – 3062-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolaseAdd BLAST306

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.1 Publication

Protein-protein interaction databases

STRINGi768679.TTX_1156a.

Structurei

Secondary structure

1306
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi22 – 26Combined sources5
Helixi38 – 50Combined sources13
Beta strandi55 – 58Combined sources4
Turni61 – 64Combined sources4
Helixi65 – 67Combined sources3
Helixi70 – 83Combined sources14
Beta strandi85 – 90Combined sources6
Helixi96 – 108Combined sources13
Beta strandi112 – 116Combined sources5
Helixi127 – 140Combined sources14
Beta strandi145 – 149Combined sources5
Helixi151 – 154Combined sources4
Helixi160 – 166Combined sources7
Beta strandi169 – 174Combined sources6
Helixi179 – 188Combined sources10
Beta strandi192 – 196Combined sources5
Helixi199 – 201Combined sources3
Helixi202 – 207Combined sources6
Beta strandi211 – 213Combined sources3
Helixi216 – 218Combined sources3
Helixi222 – 233Combined sources12
Helixi237 – 257Combined sources21
Helixi259 – 271Combined sources13
Helixi287 – 296Combined sources10
Helixi298 – 302Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R91X-ray2.00A/B/C/D21-306[»]
2R94X-ray2.20A/B/C/D21-306[»]
ProteinModelPortaliQ704D1.
SMRiQ704D1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ704D1.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni61 – 62Substrate binding2
Regioni148 – 150Substrate bindingCurated3
Regioni173 – 175Substrate binding3

Sequence similaritiesi

Belongs to the DapA family. KDPG aldolase subfamily.Curated

Phylogenomic databases

eggNOGiarCOG04172. Archaea.
COG0329. LUCA.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002220. DapA-like.
[Graphical view]
PANTHERiPTHR12128. PTHR12128. 1 hit.
PfamiPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFiPIRSF001365. DHDPS. 1 hit.
PRINTSiPR00146. DHPICSNTHASE.
SMARTiSM01130. DHDPS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q704D1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHPLIPFRA NFLRAPRVLS MEIVAPVITT FRGGRLDPEL FANHVKNITS
60 70 80 90 100
KGVDVVFVAG TTGLGPALSL QEKMELTDAA TSAARRVIVQ VASLNADEAI
110 120 130 140 150
ALAKYAESRG AEAVASLPPY YFPRLSERQI AKYFRDLCSA VSIPVFLYNY
160 170 180 190 200
PAAVGRDVDA RAAKELGCIR GVKDTNESLA HTLAYKRYLP QARVYNGSDS
210 220 230 240 250
LVFASFAVRL DGVVASSANY LPELLAGIRD AVAAGDIERA RSLQFLLDEI
260 270 280 290 300
VESARHIGYA AAVYELVEIF QGYEAGEPRG PVYPLDPEEK AWLRAAVAKA

KSQLRL
Length:306
Mass (Da):33,287
Last modified:July 5, 2004 - v1
Checksum:i8F895D811AD8EDB8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ621282 Genomic DNA. Translation: CAF18463.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ621282 Genomic DNA. Translation: CAF18463.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R91X-ray2.00A/B/C/D21-306[»]
2R94X-ray2.20A/B/C/D21-306[»]
ProteinModelPortaliQ704D1.
SMRiQ704D1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi768679.TTX_1156a.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiarCOG04172. Archaea.
COG0329. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00856; UER00829.
BRENDAi4.1.2.14. 6329.

Miscellaneous databases

EvolutionaryTraceiQ704D1.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002220. DapA-like.
[Graphical view]
PANTHERiPTHR12128. PTHR12128. 1 hit.
PfamiPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFiPIRSF001365. DHDPS. 1 hit.
PRINTSiPR00146. DHPICSNTHASE.
SMARTiSM01130. DHDPS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKDGA_THETE
AccessioniPrimary (citable) accession number: Q704D1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2013
Last sequence update: July 5, 2004
Last modified: November 2, 2016
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.