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Protein

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

Gene

Saci_0225

Organism
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
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).1 Publication

Catalytic activityi

2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate.1 Publication
2-dehydro-3-deoxy-6-phospho-D-galactonate = pyruvate + D-glyceraldehyde 3-phosphate.1 Publication

Kineticsi

  1. KM=1.1 mM for pyruvate (at pH 6 and at 70 degrees Celsius)1 Publication
  2. KM=6.3 mM for D-glyceraldehyde (at pH 6 and at 70 degrees Celsius)1 Publication
  1. Vmax=26.3 µmol/min/mg enzyme with pyruvate as substrate (at pH 6 and at 70 degrees Celsius)1 Publication
  2. Vmax=33.1 µmol/min/mg enzyme with D-glyceraldehyde as substrate (at pH 6 and at 70 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 6.5.1 Publication

Temperature dependencei

Optimum temperature is around 99 degrees Celsius. Extremely thermostable.1 Publication

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 (Saci_0225)
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
Sitei129Proton shuttleBy similarity1
Active sitei153Schiff-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

BioCyciSACI330779:GH9J-223-MONOMER.
BRENDAi4.1.2.55. 6160.
UniPathwayiUPA00856; UER00829.

Names & Taxonomyi

Protein namesi
Recommended name:
2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase (EC:4.1.2.551 Publication)
Gene namesi
Ordered Locus Names:Saci_0225
OrganismiSulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Taxonomic identifieri330779 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
Proteomesi
  • UP000001018 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004226561 – 2882-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolaseAdd BLAST288

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.1 Publication

Protein-protein interaction databases

STRINGi330779.Saci_0225.

Structurei

Secondary structure

1288
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi19 – 31Combined sources13
Beta strandi36 – 39Combined sources4
Turni42 – 45Combined sources4
Helixi46 – 48Combined sources3
Helixi51 – 61Combined sources11
Turni62 – 64Combined sources3
Beta strandi68 – 71Combined sources4
Helixi77 – 88Combined sources12
Beta strandi93 – 97Combined sources5
Helixi108 – 121Combined sources14
Beta strandi126 – 130Combined sources5
Helixi132 – 135Combined sources4
Helixi141 – 144Combined sources4
Turni145 – 148Combined sources4
Beta strandi149 – 154Combined sources6
Helixi159 – 168Combined sources10
Beta strandi173 – 176Combined sources4
Helixi179 – 181Combined sources3
Helixi182 – 186Combined sources5
Beta strandi189 – 193Combined sources5
Helixi195 – 198Combined sources4
Helixi201 – 212Combined sources12
Helixi216 – 234Combined sources19
Helixi238 – 250Combined sources13
Helixi266 – 286Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NUWX-ray1.80A/B1-288[»]
2NUXX-ray2.50A/B1-288[»]
2NUYX-ray2.50A/B1-288[»]
ProteinModelPortaliQ4JC35.
SMRiQ4JC35.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ4JC35.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni42 – 43Substrate binding2
Regioni129 – 131Substrate bindingBy similarity3
Regioni153 – 155Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the DapA family. KDPG aldolase subfamily.Curated

Phylogenomic databases

eggNOGiarCOG04172. Archaea.
COG0329. LUCA.
HOGENOMiHOG000268172.
KOiK11395.
OMAiQFGELFN.

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.

Q4JC35-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIISPIITP FDKQGKVNVD ALKTHAKNLL EKGIDAIFVN GTTGLGPALS
60 70 80 90 100
KDEKRQNLNA LYDVTHKLIF QVGSLNLNDV MELVKFSNEM DILGVSSHSP
110 120 130 140 150
YYFPRLPEKF LAKYYEEIAR ISSHSLYIYN YPAATGYDIP PSILKSLPVK
160 170 180 190 200
GIKDTNQDLA HSLEYKLNLP GVKVYNGSNT LIYYSLLSLD GVVASFTNFI
210 220 230 240 250
PEVIVKQRDL IKQGKLDDAL RLQELINRLA DILRKYGSIS AIYVLVNEFQ
260 270 280
GYDVGYPRPP IFPLTDEEAL SLKREIEPLK RKIQELVH
Length:288
Mass (Da):32,516
Last modified:August 2, 2005 - v1
Checksum:i131D33E25C9ACC78
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000077 Genomic DNA. Translation: AAY79644.1.
RefSeqiWP_011277145.1. NC_007181.1.

Genome annotation databases

EnsemblBacteriaiAAY79644; AAY79644; Saci_0225.
GeneIDi3474365.
KEGGisai:Saci_0225.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000077 Genomic DNA. Translation: AAY79644.1.
RefSeqiWP_011277145.1. NC_007181.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NUWX-ray1.80A/B1-288[»]
2NUXX-ray2.50A/B1-288[»]
2NUYX-ray2.50A/B1-288[»]
ProteinModelPortaliQ4JC35.
SMRiQ4JC35.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi330779.Saci_0225.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAY79644; AAY79644; Saci_0225.
GeneIDi3474365.
KEGGisai:Saci_0225.

Phylogenomic databases

eggNOGiarCOG04172. Archaea.
COG0329. LUCA.
HOGENOMiHOG000268172.
KOiK11395.
OMAiQFGELFN.

Enzyme and pathway databases

UniPathwayiUPA00856; UER00829.
BioCyciSACI330779:GH9J-223-MONOMER.
BRENDAi4.1.2.55. 6160.

Miscellaneous databases

EvolutionaryTraceiQ4JC35.

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_SULAC
AccessioniPrimary (citable) accession number: Q4JC35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2013
Last sequence update: August 2, 2005
Last modified: November 2, 2016
This is version 67 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, Complete proteome, Reference proteome

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.