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P00885 (ALKD_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:eda
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length226 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homotrimer.

Sequence similarities

Belongs to the KHG/KDPG aldolase family.

Ontologies

Keywords
   LigandSchiff base
   Molecular functionLyase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Molecular_function2-dehydro-3-deoxy-phosphogluconate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 2262252-dehydro-3-deoxy-phosphogluconate aldolase
PRO_0000201035

Sites

Active site611
Active site1451Schiff-base intermediate with substrate Ref.2

Experimental info

Sequence conflict1101E → Q in CAC14910. Ref.1
Sequence conflict195 – 1962TG → GT in CAC14910. Ref.1
Sequence conflict2201I → M in CAC14910. Ref.1

Secondary structure

........................................ 226
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00885 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 081FE3492F7A1452

FASTA22624,069
        10         20         30         40         50         60 
MTTLERPQPK LSMADKAARI DAICEKARIL PVITIAREED ILPLADALAA GGIRTLEVTL 

        70         80         90        100        110        120 
RSQHGLKAIQ VLREQRPELC VGAGTVLDRS MFAAVEAAGA QFVVTPGITE DILEAGVDSE 

       130        140        150        160        170        180 
IPLLPGISTP SEIMMGYALG YRRFKLFPAE ISGGVAAIKA FGGPFGDIRF CPTGGVNPAN 

       190        200        210        220 
VRNYMALPNV MCVGTGWMLD SSWIKNGDWA RIEACSAEAI ALLDAN 

« Hide

References

[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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ279003 Genomic DNA. Translation: CAC14910.1.
PIRADPSGP. A01105.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MXSX-ray2.20A2-225[»]
ProteinModelPortalP00885.
SMRP00885. Positions 11-226.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR000887. Aldlse_KDPG_KHG.
IPR013785. Aldolase_TIM.
[Graphical view]
PfamPF01081. Aldolase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01182. eda. 1 hit.
PROSITEPS00159. ALDOLASE_KDPG_KHG_1. 1 hit.
PS00160. ALDOLASE_KDPG_KHG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00885.

Entry information

Entry nameALKD_PSEPU
AccessionPrimary (citable) accession number: P00885
Secondary accession number(s): Q9EV78
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references