ALKH_SHIFL
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 03-AUG-2022, entry version 103.
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; Proteobacteria; 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}.
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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 EnsemblBacteria; AAN43418; AAN43418; SF1860.
DR EnsemblBacteria; AAP17241; AAP17241; S1926.
DR GeneID; 1025033; -.
DR GeneID; 66674260; -.
DR KEGG; sfl:SF1860; -.
DR KEGG; sfx:S1926; -.
DR PATRIC; fig|198214.7.peg.2216; -.
DR HOGENOM; CLU_077795_1_1_6; -.
DR OMA; FFPAEYC; -.
DR OrthoDB; 1497385at2; -.
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; -; 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 PANTHER; PTHR30246; PTHR30246; 1.
DR Pfam; PF01081; Aldolase; 1.
DR TIGRFAMs; TIGR01182; eda; 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
