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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)DescriptionActionsGraphical viewLength
Active sitei611
Active sitei145Schiff-base intermediate with substratePROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

GO - Biological processi

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002010352 – 2262-dehydro-3-deoxy-phosphogluconate aldolaseAdd BLAST225

Interactioni

Subunit structurei

Homotrimer.

Protein-protein interaction databases

STRINGi160488.PP_1024.

Structurei

Secondary structure

1226
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 27Combined sources15
Beta strandi28 – 33Combined sources6
Helixi38 – 40Combined sources3
Helixi41 – 50Combined sources10
Beta strandi55 – 62Combined sources8
Helixi65 – 75Combined sources11
Beta strandi79 – 84Combined sources6
Helixi89 – 98Combined sources10
Beta strandi101 – 104Combined sources4
Helixi110 – 118Combined sources9
Helixi130 – 137Combined sources8
Turni138 – 140Combined sources3
Beta strandi143 – 146Combined sources4
Helixi149 – 152Combined sources4
Helixi154 – 162Combined sources9
Turni163 – 167Combined sources5
Beta strandi169 – 175Combined sources7
Turni178 – 180Combined sources3
Helixi181 – 186Combined sources6
Beta strandi193 – 195Combined sources3
Helixi201 – 205Combined sources5
Helixi209 – 221Combined sources13

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP00885.

Family & Domainsi

Sequence similaritiesi

Belongs to the KHG/KDPG aldolase family.Curated

Phylogenomic databases

eggNOGiENOG4108UHU. Bacteria.
COG0800. LUCA.

Family and domain databases

CDDicd00452. KDPG_aldolase. 1 hit.
Gene3Di3.20.20.70. 1 hit.
InterProiIPR000887. Aldlse_KDPG_KHG.
IPR013785. Aldolase_TIM.
IPR031337. KDPG/KHG_AS_1.
IPR031338. KDPG/KHG_AS_2.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti110E → Q in CAC14910 (PubMed:12393206).Curated1
Sequence conflicti195 – 196TG → GT in CAC14910 (PubMed:12393206).Curated2
Sequence conflicti220I → M in CAC14910 (PubMed:12393206).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MXSX-ray2.20A2-226[»]
ProteinModelPortaliP00885.
SMRiP00885.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi160488.PP_1024.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108UHU. Bacteria.
COG0800. LUCA.

Miscellaneous databases

EvolutionaryTraceiP00885.

Family and domain databases

CDDicd00452. KDPG_aldolase. 1 hit.
Gene3Di3.20.20.70. 1 hit.
InterProiIPR000887. Aldlse_KDPG_KHG.
IPR013785. Aldolase_TIM.
IPR031337. KDPG/KHG_AS_1.
IPR031338. KDPG/KHG_AS_2.
[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...

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 2, 2016
This is version 91 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

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.