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Protein

2-dehydro-3-deoxy-phosphogluconate aldolase

Gene

eda

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei61 – 611
Active sitei145 – 1451Schiff-base intermediate with substrate1 PublicationPROSITE-ProRule annotation

GO - Molecular functioni

  1. 2-dehydro-3-deoxy-phosphogluconate aldolase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Schiff base

Names & Taxonomyi

Protein namesi
Recommended name:
2-dehydro-3-deoxy-phosphogluconate aldolase (EC:4.1.2.14)
Alternative name(s):
KDPG-aldolase
Phospho-2-dehydro-3-deoxygluconate aldolase
Phospho-2-keto-3-deoxygluconate aldolase
Gene namesi
Name:eda
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 2262252-dehydro-3-deoxy-phosphogluconate aldolasePRO_0000201035Add
BLAST

Interactioni

Subunit structurei

Homotrimer.

Structurei

Secondary structure

1
226
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 2715Combined sources
Beta strandi28 – 336Combined sources
Helixi38 – 403Combined sources
Helixi41 – 5010Combined sources
Beta strandi55 – 628Combined sources
Helixi65 – 7511Combined sources
Beta strandi79 – 846Combined sources
Helixi89 – 9810Combined sources
Beta strandi101 – 1044Combined sources
Helixi110 – 1189Combined sources
Helixi130 – 1378Combined sources
Turni138 – 1403Combined sources
Beta strandi143 – 1464Combined sources
Helixi149 – 1524Combined sources
Helixi154 – 1629Combined sources
Turni163 – 1675Combined sources
Beta strandi169 – 1757Combined sources
Turni178 – 1803Combined sources
Helixi181 – 1866Combined sources
Beta strandi193 – 1953Combined sources
Helixi201 – 2055Combined sources
Helixi209 – 22113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MXSX-ray2.20A2-226[»]
ProteinModelPortaliP00885.
SMRiP00885. Positions 11-226.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00885.

Family & Domainsi

Sequence similaritiesi

Belongs to the KHG/KDPG aldolase family.Curated

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR000887. Aldlse_KDPG_KHG.
IPR013785. Aldolase_TIM.
[Graphical view]
PfamiPF01081. Aldolase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01182. eda. 1 hit.
PROSITEiPS00159. ALDOLASE_KDPG_KHG_1. 1 hit.
PS00160. ALDOLASE_KDPG_KHG_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00885-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTLERPQPK LSMADKAARI DAICEKARIL PVITIAREED ILPLADALAA
60 70 80 90 100
GGIRTLEVTL RSQHGLKAIQ VLREQRPELC VGAGTVLDRS MFAAVEAAGA
110 120 130 140 150
QFVVTPGITE DILEAGVDSE IPLLPGISTP SEIMMGYALG YRRFKLFPAE
160 170 180 190 200
ISGGVAAIKA FGGPFGDIRF CPTGGVNPAN VRNYMALPNV MCVGTGWMLD
210 220
SSWIKNGDWA RIEACSAEAI ALLDAN
Length:226
Mass (Da):24,069
Last modified:January 23, 2007 - v2
Checksum:i081FE3492F7A1452
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1101E → Q in CAC14910. (PubMed:12393206)Curated
Sequence conflicti195 – 1962TG → GT in CAC14910. (PubMed:12393206)Curated
Sequence conflicti220 – 2201I → M in CAC14910. (PubMed:12393206)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ279003 Genomic DNA. Translation: CAC14910.1.
PIRiA01105. ADPSGP.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ279003 Genomic DNA. Translation: CAC14910.1.
PIRiA01105. ADPSGP.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MXSX-ray2.20A2-226[»]
ProteinModelPortaliP00885.
SMRiP00885. Positions 11-226.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00885.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR000887. Aldlse_KDPG_KHG.
IPR013785. Aldolase_TIM.
[Graphical view]
PfamiPF01081. Aldolase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01182. eda. 1 hit.
PROSITEiPS00159. ALDOLASE_KDPG_KHG_1. 1 hit.
PS00160. ALDOLASE_KDPG_KHG_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Analysis of the zwf-pgl-eda-operon in Pseudomonas putida strains H and KT2440."
    Petruschka L., Adolf K., Burchhardt G., Dernedde J., Jurgensen J., Herrmann H.
    FEMS Microbiol. Lett. 215:89-95(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: H.
  2. "Complete primary structure of 2-keto-3-deoxy-6-phosphogluconate aldolase."
    Suzuki N., Wood W.A.
    J. Biol. Chem. 255:3427-3435(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-226.
  3. "Structure of 2-keto-3-deoxy-6-phosphogluconate aldolase at 2.8-A resolution."
    Mavridis I.M., Hatada M.H., Tulinsky A., Lebioda L.
    J. Mol. Biol. 162:419-444(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  4. "The folding and quaternary structure of trimeric 2-keto-3-deoxy-6-phosphogluconic aldolase at 3.5-A resolution."
    Mavridis I.M., Tulinsky A.
    Biochemistry 15:4410-4417(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).

Entry informationi

Entry nameiALKD_PSEPU
AccessioniPrimary (citable) accession number: P00885
Secondary accession number(s): Q9EV78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.