KDGA_PICTO
ID KDGA_PICTO Reviewed; 266 AA.
AC Q6KZI8;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolase;
DE EC=4.1.2.14 {ECO:0000269|PubMed:20023024};
DE EC=4.1.2.51 {ECO:0000269|PubMed:20023024};
DE AltName: Full=2-dehydro-3-deoxy-galactonate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase;
DE EC=4.1.2.- {ECO:0000269|PubMed:20023024};
DE EC=4.1.2.21 {ECO:0000269|PubMed:20023024};
GN OrderedLocusNames=PTO1279;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
RN [2]
RP PROTEIN SEQUENCE OF 1-37, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=20023024; DOI=10.1128/jb.01281-09;
RA Reher M., Fuhrer T., Bott M., Schonheit P.;
RT "The nonphosphorylative Entner-Doudoroff pathway in the thermoacidophilic
RT euryarchaeon Picrophilus torridus involves a novel 2-keto-3-deoxygluconate-
RT specific aldolase.";
RL J. Bacteriol. 192:964-974(2010).
CC -!- FUNCTION: Involved in the degradation of glucose via the Entner-
CC Doudoroff pathway. Catalyzes the reversible cleavage of 2-keto-3-deoxy-
CC 6-phosphogluconate (KDPG) and 2-keto-3-deoxygluconate (KDG) forming
CC pyruvate and glyceraldehyde 3-phosphate or glyceraldehyde,
CC respectively. It is also able to catalyze the reversible cleavage of 2-
CC keto-3-deoxy-6-phosphogalactonate (KDPGal) and 2-keto-3-
CC deoxygalactonate (KDGal). It is equally active with both D- and L-
CC glyceraldehyde. {ECO:0000269|PubMed:20023024}.
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 Evidence={ECO:0000269|PubMed:20023024};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-D-gluconate = D-glyceraldehyde + pyruvate;
CC Xref=Rhea:RHEA:35583, ChEBI:CHEBI:15361, ChEBI:CHEBI:17378,
CC ChEBI:CHEBI:57990; EC=4.1.2.51;
CC Evidence={ECO:0000269|PubMed:20023024};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-6-phospho-D-galactonate = D-glyceraldehyde
CC 3-phosphate + pyruvate; Xref=Rhea:RHEA:24464, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:58298, ChEBI:CHEBI:59776; EC=4.1.2.21;
CC Evidence={ECO:0000269|PubMed:20023024};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-D-galactonate = D-glyceraldehyde + pyruvate;
CC Xref=Rhea:RHEA:46116, ChEBI:CHEBI:15361, ChEBI:CHEBI:17378,
CC ChEBI:CHEBI:57989; Evidence={ECO:0000269|PubMed:20023024};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 mM for KDG (at 60 degrees Celsius and pH 6.2)
CC {ECO:0000269|PubMed:20023024};
CC KM=2.7 mM for pyruvate (at 60 degrees Celsius and pH 6.2)
CC {ECO:0000269|PubMed:20023024};
CC KM=4.6 mM for glyceraldehyde (at 60 degrees Celsius and pH 6.2)
CC {ECO:0000269|PubMed:20023024};
CC KM=8 mM for KDPG (at 60 degrees Celsius and pH 6.2)
CC {ECO:0000269|PubMed:20023024};
CC Vmax=67 umol/min/mg enzyme with KDG as D-glyceraldehyde (at 60
CC degrees Celsius and pH 6.2) {ECO:0000269|PubMed:20023024};
CC Vmax=59 umol/min/mg enzyme with KDG as L-glyceraldehyde (at 60
CC degrees Celsius and pH 6.2) {ECO:0000269|PubMed:20023024};
CC Vmax=50 umol/min/mg enzyme with KDG as substrate (at 60 degrees
CC Celsius and pH 6.2) {ECO:0000269|PubMed:20023024};
CC Vmax=0.63 umol/min/mg enzyme with KDPG as substrate (at 60 degrees
CC Celsius and pH 6.2) {ECO:0000269|PubMed:20023024};
CC pH dependence:
CC Optimum pH is 5.5, and 50% of activity is found at pH 4.5 and 7.5.
CC {ECO:0000269|PubMed:20023024};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius. It shows high
CC thermostability. At 70 degrees Celsius, the enzyme does not lose
CC activity upon incubation for 2 hours. The half-lives of the enzyme at
CC 80 degrees Celsius and 90 degrees Celsius are 20 minutes and 15
CC minutes, respectively. {ECO:0000269|PubMed:20023024};
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 -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000305|PubMed:20023024}.
CC -!- SIMILARITY: Belongs to the DapA family. KDPG aldolase subfamily.
CC {ECO:0000305}.
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DR EMBL; AE017261; AAT43864.1; -; Genomic_DNA.
DR PDB; 4UXD; X-ray; 2.50 A; A/B/C/D=1-266.
DR PDBsum; 4UXD; -.
DR AlphaFoldDB; Q6KZI8; -.
DR SMR; Q6KZI8; -.
DR STRING; 263820.PTO1279; -.
DR PRIDE; Q6KZI8; -.
DR EnsemblBacteria; AAT43864; AAT43864; PTO1279.
DR KEGG; pto:PTO1279; -.
DR eggNOG; arCOG04172; Archaea.
DR HOGENOM; CLU_049343_5_1_2; -.
DR OMA; GMDACVP; -.
DR BRENDA; 4.1.2.51; 7518.
DR UniPathway; UPA00856; UER00829.
DR Proteomes; UP000000438; Chromosome.
DR GO; GO:0008674; F:2-dehydro-3-deoxy-6-phosphogalactonate aldolase activity; IDA:UniProtKB.
DR GO; GO:0061677; F:2-dehydro-3-deoxy-D-gluconate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008675; F:2-dehydro-3-deoxy-phosphogluconate aldolase activity; IDA:UniProtKB.
DR GO; GO:0016832; F:aldehyde-lyase activity; IDA:UniProtKB.
DR GO; GO:0006007; P:glucose catabolic process; IDA:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR PANTHER; PTHR12128; PTHR12128; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR PROSITE; PS00666; DHDPS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing; Lyase;
KW Reference proteome; Schiff base.
FT CHAIN 1..266
FT /note="2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-
FT phosphogluconate aldolase"
FT /id="PRO_0000422659"
FT ACT_SITE 151
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT BINDING 36..37
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 123..125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 151..153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 123
FT /note="Proton shuttle"
FT /evidence="ECO:0000250"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:4UXD"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:4UXD"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:4UXD"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:4UXD"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4UXD"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:4UXD"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:4UXD"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:4UXD"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:4UXD"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:4UXD"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:4UXD"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:4UXD"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:4UXD"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:4UXD"
FT HELIX 157..164
FT /evidence="ECO:0007829|PDB:4UXD"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:4UXD"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:4UXD"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:4UXD"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:4UXD"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:4UXD"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:4UXD"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:4UXD"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:4UXD"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:4UXD"
FT HELIX 239..248
FT /evidence="ECO:0007829|PDB:4UXD"
SQ SEQUENCE 266 AA; 30391 MW; B2B038281D4869E8 CRC64;
MITPLDAHGN IDYNATNILI KYLEGINVDY LFPMGSTGVF PYFTLKERKD FLKFVRENSK
KPIMAGVGSS SINEVNELMK FSMDIGIEAA VLMPPYYIKL NQEAIYHYYK EILSSNDMDL
LIYNIPQFTN KIDPETVKNL KSEFSSVKGV KDSSADIRGF MEMLSLSDDD FAVFQGQDDL
LFTSLELGAS GGVCGTTNFS DGIVRLYHEY KNNREMALKI EKNDVIPLMK KLGKYQFPNA
YYEYFYKKNN INGGYRPPMY RVGIEI
