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Protein

2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase

Gene
N/A
Organism
Sulfolobus solfataricus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the degradation of glucose and galactose 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.3 Publications

Catalytic activityi

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

Kineticsi

Kcat is 28.2 (sec-1) for KDG and 6.8 (sec-1) for KDGal.

  1. KM=0.1 mM for KDPG (at 60 degrees Celsius and at pH 6)3 Publications
  2. KM=0.17 mM for KDPGal (at 60 degrees Celsius and at pH 6)3 Publications
  3. KM=3.9 mM for pyruvate (at 70 degrees Celsius and at pH 6)3 Publications
  4. KM=3.9 mM for D-glyceraldehyde (at 70 degrees Celsius and at pH 6)3 Publications
  5. KM=5.2 mM for D,L-glyceraldehyde (at 70 degrees Celsius and at pH 6)3 Publications
  6. KM=7.1 mM for L-glyceraldehyde (at 70 degrees Celsius and at pH 6)3 Publications
  7. KM=9.9 mM for KDGal (at 60 degrees Celsius and at pH 6)3 Publications
  8. KM=25.7 mM for KDG (at 60 degrees Celsius and at pH 6)3 Publications
  1. Vmax=12.3 µmol/min/mg enzyme with KDGal as substrate (at 60 degrees Celsius and at pH 6)3 Publications
  2. Vmax=15.7 µmol/min/mg enzyme with pyruvate as substrate (at 70 degrees Celsius and at pH 6)3 Publications
  3. Vmax=17.1 µmol/min/mg enzyme with D,L-glyceraldehyde as substrate (at 70 degrees Celsius and at pH 6)3 Publications
  4. Vmax=18 µmol/min/mg enzyme with D-glyceraldehyde as substrate (at 70 degrees Celsius and at pH 6)3 Publications
  5. Vmax=18 µmol/min/mg enzyme with L-glyceraldehyde as substrate (at 70 degrees Celsius and at pH 6)3 Publications
  6. Vmax=51.4 µmol/min/mg enzyme with KDG as substrate (at 60 degrees Celsius and at pH 6)3 Publications

Temperature dependencei

Extremely thermostable.3 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. no protein annotated in this organism
  2. 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase
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
Sitei130Proton shuttleBy similarity1
Active sitei155Schiff-base intermediate with substrate1 Publication1

GO - Molecular functioni

  • 2-dehydro-3-deoxy-6-phosphogalactonate aldolase activity Source: UniProtKB
  • 2-dehydro-3-deoxy-phosphogluconate aldolase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-4861.
BRENDAi4.1.2.55. 6163.
SABIO-RKO54288.
UniPathwayiUPA00856; UER00829.

Names & Taxonomyi

Protein namesi
Recommended name:
2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase (EC:4.1.2.552 Publications)
OrganismiSulfolobus solfataricus
Taxonomic identifieri2287 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00004226582 – 2942-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolaseAdd BLAST293

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.3 Publications

Protein-protein interaction databases

STRINGi273057.SSO3197.

Structurei

Secondary structure

1294
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 7Combined sources5
Beta strandi16 – 18Combined sources3
Helixi20 – 32Combined sources13
Beta strandi37 – 42Combined sources6
Turni43 – 46Combined sources4
Helixi47 – 49Combined sources3
Helixi52 – 63Combined sources12
Beta strandi69 – 72Combined sources4
Helixi78 – 87Combined sources10
Helixi88 – 90Combined sources3
Beta strandi94 – 99Combined sources6
Helixi109 – 122Combined sources14
Beta strandi127 – 131Combined sources5
Helixi133 – 136Combined sources4
Helixi142 – 148Combined sources7
Beta strandi151 – 156Combined sources6
Helixi161 – 170Combined sources10
Beta strandi174 – 178Combined sources5
Helixi181 – 183Combined sources3
Helixi184 – 189Combined sources6
Beta strandi194 – 196Combined sources3
Helixi198 – 201Combined sources4
Helixi204 – 215Combined sources12
Helixi219 – 237Combined sources19
Helixi241 – 253Combined sources13
Helixi269 – 288Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W37X-ray2.00A/B/C/D1-294[»]
1W3IX-ray1.70A/B/C/D2-294[»]
1W3NX-ray2.10A/B/C/D1-294[»]
1W3TX-ray2.10A/B/C/D1-294[»]
2YDAX-ray1.91A/B1-294[»]
ProteinModelPortaliO54288.
SMRiO54288.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO54288.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni43 – 44Substrate binding2
Regioni130 – 132Substrate binding3
Regioni155 – 157Substrate binding3

Sequence similaritiesi

Belongs to the DapA family. KDPG aldolase subfamily.Curated

Phylogenomic databases

eggNOGiarCOG04172. Archaea.
COG0329. LUCA.
KOiK11395.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

O54288-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEIITPIIT PFTKDNRIDK EKLKIHAENL IRKGIDKLFV NGTTGLGPSL
60 70 80 90 100
SPEEKLENLK AVYDVTNKII FQVGGLNLDD AIRLAKLSKD FDIVGIASYA
110 120 130 140 150
PYYYPRMSEK HLVKYFKTLC EVSPHPVYLY NYPTATGKDI DAKVAKEIGC
160 170 180 190 200
FTGVKDTIEN IIHTLDYKRL NPNMLVYSGS DMLIATVAST GLDGNVAAGS
210 220 230 240 250
NYLPEVTVTI KKLAMERKID EALKLQFLHD EVIEASRIFG SLSSNYVLTK
260 270 280 290
YFQGYDLGYP RPPIFPLDDE EERQLIKKVE GIRAKLVELK ILKE
Length:294
Mass (Da):33,108
Last modified:June 1, 1998 - v1
Checksum:iD709A94ACF68B0EF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ224174 Genomic DNA. Translation: CAA11866.1.
RefSeqiWP_009991687.1. NZ_LT549890.1.

Genome annotation databases

GeneIDi27429444.
KEGGiag:CAA11866.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ224174 Genomic DNA. Translation: CAA11866.1.
RefSeqiWP_009991687.1. NZ_LT549890.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W37X-ray2.00A/B/C/D1-294[»]
1W3IX-ray1.70A/B/C/D2-294[»]
1W3NX-ray2.10A/B/C/D1-294[»]
1W3TX-ray2.10A/B/C/D1-294[»]
2YDAX-ray1.91A/B1-294[»]
ProteinModelPortaliO54288.
SMRiO54288.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273057.SSO3197.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi27429444.
KEGGiag:CAA11866.

Phylogenomic databases

eggNOGiarCOG04172. Archaea.
COG0329. LUCA.
KOiK11395.

Enzyme and pathway databases

UniPathwayiUPA00856; UER00829.
BioCyciMetaCyc:MONOMER-4861.
BRENDAi4.1.2.55. 6163.
SABIO-RKO54288.

Miscellaneous databases

EvolutionaryTraceiO54288.

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_SULSF
AccessioniPrimary (citable) accession number: O54288
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2013
Last sequence update: June 1, 1998
Last modified: November 2, 2016
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The metabolic pathway in Sulfolobus species contrasts with the situation observed in other microorganisms where separate enzymes exist for the catabolism of the two sugars, glucose and galactose.1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.