ID   ALKH_ECOL6              Reviewed;         213 AA.
AC   P0A956; P10177;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=KHG/KDPG aldolase;
DE   Includes:
DE     RecName: Full=4-hydroxy-2-oxoglutarate aldolase;
DE              EC=4.1.3.16;
DE     AltName: Full=2-keto-4-hydroxyglutarate aldolase;
DE              Short=KHG-aldolase;
DE   Includes:
DE     RecName: Full=2-dehydro-3-deoxy-phosphogluconate aldolase;
DE              EC=4.1.2.14;
DE     AltName: Full=2-keto-3-deoxy-6-phosphogluconate aldolase;
DE              Short=KDPG-aldolase;
DE     AltName: Full=Phospho-2-dehydro-3-deoxygluconate aldolase;
DE     AltName: Full=Phospho-2-keto-3-deoxygluconate aldolase;
GN   Name=eda; OrderedLocusNames=c2263;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4S)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate;
CC         Xref=Rhea:RHEA:35639, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:71685; EC=4.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4R)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate;
CC         Xref=Rhea:RHEA:30687, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:62213; EC=4.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-dehydro-3-deoxy-6-phospho-D-gluconate = D-glyceraldehyde 3-
CC         phosphate + pyruvate; Xref=Rhea:RHEA:17089, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:57569, ChEBI:CHEBI:59776; EC=4.1.2.14;
CC   -!- PATHWAY: Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D-gluconate
CC       degradation; D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-
CC       3-deoxy-D-gluconate: step 2/2.
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate and dicarboxylate
CC       metabolism.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: It also catalyzes the beta-decarboxylation of
CC       oxaloacetate. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the KHG/KDPG aldolase family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN80720.1; -; Genomic_DNA.
DR   RefSeq; WP_000800512.1; NZ_CP051263.1.
DR   AlphaFoldDB; P0A956; -.
DR   SMR; P0A956; -.
DR   STRING; 199310.c2263; -.
DR   GeneID; 83576924; -.
DR   KEGG; ecc:c2263; -.
DR   eggNOG; COG0800; Bacteria.
DR   HOGENOM; CLU_077795_1_1_6; -.
DR   BioCyc; ECOL199310:C2263-MONOMER; -.
DR   UniPathway; UPA00227; -.
DR   UniPathway; UPA00856; UER00829.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0106009; F:(4S)-4-hydroxy-2-oxoglutarate aldolase activity; IEA:RHEA.
DR   GO; GO:0008675; F:2-dehydro-3-deoxy-phosphogluconate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008700; F:4-hydroxy-2-oxoglutarate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00452; KDPG_aldolase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR000887; Aldlse_KDPG_KHG.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR031337; KDPG/KHG_AS_1.
DR   InterPro; IPR031338; KDPG/KHG_AS_2.
DR   NCBIfam; TIGR01182; eda; 1.
DR   PANTHER; PTHR30246; 2-KETO-3-DEOXY-6-PHOSPHOGLUCONATE ALDOLASE; 1.
DR   PANTHER; PTHR30246:SF2; KHG_KDPG ALDOLASE; 1.
DR   Pfam; PF01081; Aldolase; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00159; ALDOLASE_KDPG_KHG_1; 1.
DR   PROSITE; PS00160; ALDOLASE_KDPG_KHG_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lyase; Multifunctional enzyme; Reference proteome; Schiff base.
FT   CHAIN           1..213
FT                   /note="KHG/KDPG aldolase"
FT                   /id="PRO_0000201039"
FT   ACT_SITE        45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10118"
FT   ACT_SITE        49
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10118"
FT   ACT_SITE        133
FT                   /note="Schiff-base intermediate with KHG or pyruvate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10118"
SQ   SEQUENCE   213 AA;  22284 MW;  CC8D51B50480D0B7 CRC64;
     MKNWKTSAES ILTTGPVVPV IVVKKLEHAV PMAKALVAGG VRVLEVTLRT ECAVDAIRAI
     AKEVPEAIVG AGTVLNPQQL AEVTEAGAQF AISPGLTEPL LKAATEGTIP LIPGISTVSE
     LMLGMDYGLK EFKFFPAEAN GGVKALQAIA GPFSQVRFCP TGGISPANYR DYLALKSVLC
     IGGSWLVPAD ALEAGDYDRI TKLAREAVEG AKL
//