ALKH_DICD3
ID ALKH_DICD3 Reviewed; 213 AA.
AC P38448; E0SB90;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, 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; Synonyms=kdgA; OrderedLocusNames=Dda3937_03573;
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=8145647; DOI=10.1111/j.1365-2958.1994.tb00290.x;
RA Hugouvieux-Cotte-Pattat N., Robert-Baudouy J.;
RT "Molecular analysis of the Erwinia chrysanthemi region containing the kdgA
RT and zwf genes.";
RL Mol. Microbiol. 11:67-75(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=21217001; DOI=10.1128/jb.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
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.
CC -!- SIMILARITY: Belongs to the KHG/KDPG aldolase family. {ECO:0000305}.
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DR EMBL; X74866; CAA52859.1; -; Genomic_DNA.
DR EMBL; CP002038; ADM98359.1; -; Genomic_DNA.
DR PIR; S37054; S37054.
DR RefSeq; WP_013317813.1; NC_014500.1.
DR AlphaFoldDB; P38448; -.
DR SMR; P38448; -.
DR STRING; 198628.Dda3937_03573; -.
DR EnsemblBacteria; ADM98359; ADM98359; Dda3937_03573.
DR GeneID; 9733589; -.
DR KEGG; ddd:Dda3937_03573; -.
DR PATRIC; fig|198628.6.peg.2135; -.
DR eggNOG; COG0800; Bacteria.
DR HOGENOM; CLU_077795_1_1_6; -.
DR OMA; FFPAEYC; -.
DR OrthoDB; 1497385at2; -.
DR BioCyc; DDAD198628:DDA3937_RS10140-MON; -.
DR BioCyc; MetaCyc:MON-15645; -.
DR UniPathway; UPA00227; -.
DR UniPathway; UPA00856; UER00829.
DR Proteomes; UP000006859; 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_0000201040"
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; 22184 MW; 641A0D1015CD7413 CRC64;
MKNWKTSAEQ ILTAGPVVPV IVINKLEHAV PMAKALVAGG VRVLELTLRT ECAVEAIRLI
AQEVPDAIVG AGTVTNPQQL AEVTAAGAQF AISPGLTEPL LKAATEGTIP LIPGISTVSE
LMLGMDYGLR EFKFFPAEAN GGVKALQAIA GPFGKIRFCP TGGISLKNYR DYLALKSVLC
VGGSWLVPAD ALESGDYDRI TALAREAVAG ATA
