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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)LengthDescriptionGraphical viewFeature identifierActions
Sitei148 – 1481Proton shuttle
Active sitei173 – 1731Schiff-base intermediate with substrate1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3063062-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolasePRO_0000422660Add
BLAST

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.1 Publication

Protein-protein interaction databases

STRINGi768679.TTX_1156a.

Structurei

Secondary structure

1
306
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 265Combined sources
Helixi38 – 5013Combined sources
Beta strandi55 – 584Combined sources
Turni61 – 644Combined sources
Helixi65 – 673Combined sources
Helixi70 – 8314Combined sources
Beta strandi85 – 906Combined sources
Helixi96 – 10813Combined sources
Beta strandi112 – 1165Combined sources
Helixi127 – 14014Combined sources
Beta strandi145 – 1495Combined sources
Helixi151 – 1544Combined sources
Helixi160 – 1667Combined sources
Beta strandi169 – 1746Combined sources
Helixi179 – 18810Combined sources
Beta strandi192 – 1965Combined sources
Helixi199 – 2013Combined sources
Helixi202 – 2076Combined sources
Beta strandi211 – 2133Combined sources
Helixi216 – 2183Combined sources
Helixi222 – 23312Combined sources
Helixi237 – 25721Combined sources
Helixi259 – 27113Combined sources
Helixi287 – 29610Combined sources
Helixi298 – 3025Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R91X-ray2.00A/B/C/D21-306[»]
2R94X-ray2.20A/B/C/D21-306[»]
ProteinModelPortaliQ704D1.
SMRiQ704D1. Positions 21-306.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ704D1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni61 – 622Substrate binding
Regioni148 – 1503Substrate bindingCurated
Regioni173 – 1753Substrate binding

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2R91X-ray2.00A/B/C/D21-306[»]
2R94X-ray2.20A/B/C/D21-306[»]
ProteinModelPortaliQ704D1.
SMRiQ704D1. Positions 21-306.
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...

Publicationsi

  1. "Reconstruction of the central carbohydrate metabolism of Thermoproteus tenax using genomic and biochemical data."
    Siebers B., Tjaden B., Michalke K., Doerr C., Ahmed H., Zaparty M., Gordon P., Sensen C.W., Zibat A., Klenk H.-P., Schuster S.C., Hensel R.
    J. Bacteriol. 186:2179-2194(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "The semi-phosphorylative Entner-Doudoroff pathway in hyperthermophilic archaea: a re-evaluation."
    Ahmed H., Ettema T.J., Tjaden B., Geerling A.C., van der Oost J., Siebers B.
    Biochem. J. 390:529-540(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
  3. "Crystal structure and stereochemical studies of KD(P)G aldolase from Thermoproteus tenax."
    Pauluhn A., Ahmed H., Lorentzen E., Buchinger S., Schomburg D., Siebers B., Pohl E.
    Proteins 72:35-43(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 21-306 IN COMPLEX WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBSTRATE SPECIFICITY, SUBUNIT.

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: May 11, 2016
This is version 49 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.