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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)LengthDescriptionGraphical viewFeature identifierActions
Sitei129 – 1291Proton shuttleBy similarity
Active sitei153 – 1531Schiff-base intermediate with substrate1 Publication

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-224-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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2882882-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolasePRO_0000422656Add
BLAST

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.1 Publication

Protein-protein interaction databases

STRINGi330779.Saci_0225.

Structurei

Secondary structure

1
288
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi19 – 3113Combined sources
Beta strandi36 – 394Combined sources
Turni42 – 454Combined sources
Helixi46 – 483Combined sources
Helixi51 – 6111Combined sources
Turni62 – 643Combined sources
Beta strandi68 – 714Combined sources
Helixi77 – 8812Combined sources
Beta strandi93 – 975Combined sources
Helixi108 – 12114Combined sources
Beta strandi126 – 1305Combined sources
Helixi132 – 1354Combined sources
Helixi141 – 1444Combined sources
Turni145 – 1484Combined sources
Beta strandi149 – 1546Combined sources
Helixi159 – 16810Combined sources
Beta strandi173 – 1764Combined sources
Helixi179 – 1813Combined sources
Helixi182 – 1865Combined sources
Beta strandi189 – 1935Combined sources
Helixi195 – 1984Combined sources
Helixi201 – 21212Combined sources
Helixi216 – 23419Combined sources
Helixi238 – 25013Combined sources
Helixi266 – 28621Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NUWX-ray1.80A/B1-288[»]
2NUXX-ray2.50A/B1-288[»]
2NUYX-ray2.50A/B1-288[»]
ProteinModelPortaliQ4JC35.
SMRiQ4JC35. Positions 1-288.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ4JC35.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni42 – 432Substrate binding
Regioni129 – 1313Substrate bindingBy similarity
Regioni153 – 1553Substrate bindingBy similarity

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2NUWX-ray1.80A/B1-288[»]
2NUXX-ray2.50A/B1-288[»]
2NUYX-ray2.50A/B1-288[»]
ProteinModelPortaliQ4JC35.
SMRiQ4JC35. Positions 1-288.
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-224-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: September 7, 2016
This is version 65 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.