Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0A957 (ALKH_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 59. 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:
KHG/KDPG aldolase

Including the following 2 domains:

  1. 4-hydroxy-2-oxoglutarate aldolase
    EC=4.1.3.16
    Alternative name(s):
    2-keto-4-hydroxyglutarate aldolase
    Short name=KHG-aldolase
  2. 2-dehydro-3-deoxy-phosphogluconate aldolase
    EC=4.1.2.14
    Alternative name(s):
    2-keto-3-deoxy-6-phosphogluconate aldolase
    Short name=KDPG-aldolase
    Phospho-2-dehydro-3-deoxygluconate aldolase
    Phospho-2-keto-3-deoxygluconate aldolase
Gene names
Name:eda
Ordered Locus Names:Z2902, ECs2560
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate.

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

Pathway

Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D-gluconate degradation; D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-gluconate: step 2/2.

Carbohydrate metabolism; glyoxylate and dicarboxylate metabolism.

Subunit structure

Homotrimer By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

It also catalyzes the beta-decarboxylation of oxaloacetate By similarity.

Sequence similarities

Belongs to the KHG/KDPG aldolase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionLyase
   Technical termComplete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function2-dehydro-3-deoxy-phosphogluconate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

4-hydroxy-2-oxoglutarate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 213213KHG/KDPG aldolase
PRO_0000201038

Sites

Active site451 By similarity
Active site491 By similarity
Active site1331Schiff-base intermediate with KHG or pyruvate By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A957 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: CC8D51B50480D0B7

FASTA21322,284
        10         20         30         40         50         60 
MKNWKTSAES ILTTGPVVPV IVVKKLEHAV PMAKALVAGG VRVLEVTLRT ECAVDAIRAI 

        70         80         90        100        110        120 
AKEVPEAIVG AGTVLNPQQL AEVTEAGAQF AISPGLTEPL LKAATEGTIP LIPGISTVSE 

       130        140        150        160        170        180 
LMLGMDYGLK EFKFFPAEAN GGVKALQAIA GPFSQVRFCP TGGISPANYR DYLALKSVLC 

       190        200        210 
IGGSWLVPAD ALEAGDYDRI TKLAREAVEG AKL 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG56840.1.
BA000007 Genomic DNA. Translation: BAB35983.1.
PIRD85797.
H90948.
RefSeqNP_288287.1. NC_002655.2.
NP_310587.1. NC_002695.1.

3D structure databases

ProteinModelPortalP0A957.
SMRP0A957. Positions 1-213.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z2902.

Proteomic databases

PRIDEP0A957.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG56840; AAG56840; Z2902.
BAB35983; BAB35983; BAB35983.
GeneID912650.
961823.
KEGGece:Z2902.
ecs:ECs2560.
PATRIC18354490. VBIEscCol44059_2456.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0800.
HOGENOMHOG000233114.
KOK01625.
OMAKFFPAEY.
OrthoDBEOG67DPKT.
ProtClustDBPRK05718.

Enzyme and pathway databases

BioCycECOL386585:GJFA-2534-MONOMER.
ECOO157:EDA-MONOMER.
UniPathwayUPA00227.
UPA00856; UER00829.

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...

Entry information

Entry nameALKH_ECO57
AccessionPrimary (citable) accession number: P0A957
Secondary accession number(s): P10177
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: December 11, 2013
This is version 59 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways