ID ALKH_SHIFL Reviewed; 213 AA. AC P0A958; P10177; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 27-MAR-2024, entry version 111. 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=SF1860, S1926; OS Shigella flexneri. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 / Serotype 2a; RX PubMed=12384590; DOI=10.1093/nar/gkf566; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella flexneri RT serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE005674; AAN43418.1; -; Genomic_DNA. DR EMBL; AE014073; AAP17241.1; -; Genomic_DNA. DR RefSeq; NP_707711.1; NC_004337.2. DR RefSeq; WP_000800512.1; NZ_WPGW01000041.1. DR AlphaFoldDB; P0A958; -. DR SMR; P0A958; -. DR STRING; 198214.SF1860; -. DR PaxDb; 198214-SF1860; -. DR GeneID; 1025033; -. DR GeneID; 83576924; -. DR KEGG; sfl:SF1860; -. DR KEGG; sfx:S1926; -. DR PATRIC; fig|198214.7.peg.2216; -. DR HOGENOM; CLU_077795_1_1_6; -. DR UniPathway; UPA00227; -. DR UniPathway; UPA00856; UER00829. DR Proteomes; UP000001006; Chromosome. DR Proteomes; UP000002673; 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_0000201042" 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 //