P00885 (ALKD_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

eda

Organism

Pseudomonas putida (Arthrobacter siderocapsulatus)

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas putida group

Protein attributes

Sequence length	226 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	2-dehydro-3-deoxy-D-gluconate 6-phosphate = pyruvate + D-glyceraldehyde 3-phosphate.
Subunit structure	Homotrimer.
Sequence similarities	Belongs to the KHG/KDPG aldolase family.

Ontologies

Keywords
Ligand	Schiff base
Molecular function	Lyase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular_function	2-dehydro-3-deoxy-phosphogluconate aldolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 226

225

2-dehydro-3-deoxy-phosphogluconate aldolase

PRO_0000201035

Sites

Active site

61

1

Active site

145

1

Schiff-base intermediate with substrate Ref.2

Experimental info

Sequence conflict

110

1

E → Q in CAC14910. Ref.1

Sequence conflict

195 – 196

2

TG → GT in CAC14910. Ref.1

Sequence conflict

220

1

I → M in CAC14910. Ref.1

Secondary structure

1

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226

Helix Strand Turn

Details...

Helix

13 – 27

15

Beta strand

28 – 33

6

Helix

38 – 40

3

Helix

41 – 50

10

Beta strand

55 – 62

8

Helix

65 – 75

11

Beta strand

79 – 84

6

Helix

89 – 98

10

Beta strand

101 – 104

4

Helix

110 – 118

9

Helix

130 – 137

8

Turn

138 – 140

3

Beta strand

143 – 146

4

Helix

149 – 152

4

Helix

154 – 162

9

Turn

163 – 167

5

Beta strand

169 – 175

7

Turn

178 – 180

3

Helix

181 – 186

6

Beta strand

193 – 195

3

Helix

201 – 205

5

Helix

209 – 221

13

Sequences

	Sequence		Length	Mass (Da)
	P00885 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 081FE3492F7A1452	FASTA	226	24,069
	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

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.

PIR

ADPSGP. A01105.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MXS	X-ray	2.20	A	2-225	[»]

ProteinModelPortal

P00885.

SMR

P00885. Positions 11-226.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR000887. Aldlse_KDPG_KHG.
IPR013785. Aldolase_TIM.
[Graphical view]

Pfam

PF01081. Aldolase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01182. eda. 1 hit.

PROSITE

PS00159. ALDOLASE_KDPG_KHG_1. 1 hit.
PS00160. ALDOLASE_KDPG_KHG_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00885.

Entry information

Entry name

ALKD_PSEPU

Accession

Primary (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:	April 3, 2013
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program