KDGA_SACSO
ID KDGA_SACSO Reviewed; 294 AA.
AC O54288;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase;
DE EC=4.1.2.55 {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170};
OS Saccharolobus solfataricus (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=2287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-39, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP AND SUBUNIT.
RC STRAIN=ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1;
RX PubMed=10527934; DOI=10.1042/bj3430563;
RA Buchanan C.L., Connaris H., Danson M.J., Reeve C.D., Hough D.W.;
RT "An extremely thermostable aldolase from Sulfolobus solfataricus with
RT specificity for non-phosphorylated substrates.";
RL Biochem. J. 343:563-570(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE STEREOSELECTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1;
RX PubMed=12824170; DOI=10.1074/jbc.m305818200;
RA Lamble H.J., Heyer N.I., Bull S.D., Hough D.W., Danson M.J.;
RT "Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus
RT revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate
RT aldolase.";
RL J. Biol. Chem. 278:34066-34072(2003).
RN [3]
RP FUNCTION, SUBSTRATE STEREOSELECTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16330030; DOI=10.1016/j.febslet.2005.11.028;
RA Lamble H.J., Theodossis A., Milburn C.C., Taylor G.L., Bull S.D.,
RA Hough D.W., Danson M.J.;
RT "Promiscuity in the part-phosphorylative Entner-Doudoroff pathway of the
RT archaeon Sulfolobus solfataricus.";
RL FEBS Lett. 579:6865-6869(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-294 IN COMPLEX WITH SUBSTRATE
RP ANALOGS, ACTIVE SITE, AND SUBUNIT.
RX PubMed=15265860; DOI=10.1074/jbc.m407702200;
RA Theodossis A., Walden H., Westwick E.J., Connaris H., Lamble H.J.,
RA Hough D.W., Danson M.J., Taylor G.L.;
RT "The structural basis for substrate promiscuity in 2-keto-3-deoxygluconate
RT aldolase from the Entner-Doudoroff pathway in Sulfolobus solfataricus.";
RL J. Biol. Chem. 279:43886-43892(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS), AND SUBUNIT.
RA Royer S.F., Crennell S.J., Angelopolou M., Hough D.W., Danson M.J.,
RA Bull S.D.;
RT "Sulfolobus sulfataricus 2-keto-3-deoxygluconate aldolase.";
RL Submitted (MAR-2011) to the PDB data bank.
CC -!- FUNCTION: Involved in the degradation of glucose and galactose via the
CC Entner-Doudoroff pathway. Catalyzes the reversible cleavage of 2-keto-
CC 3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxygluconate (KDG)
CC forming 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:10527934,
CC ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030}.
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=4.1.2.55;
CC Evidence={ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170};
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=4.1.2.55;
CC Evidence={ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 mM for KDPG (at 60 degrees Celsius and at pH 6)
CC {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170,
CC ECO:0000269|PubMed:16330030};
CC KM=0.17 mM for KDPGal (at 60 degrees Celsius and at pH 6)
CC {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170,
CC ECO:0000269|PubMed:16330030};
CC KM=3.9 mM for pyruvate (at 70 degrees Celsius and at pH 6)
CC {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170,
CC ECO:0000269|PubMed:16330030};
CC KM=3.9 mM for D-glyceraldehyde (at 70 degrees Celsius and at pH 6)
CC {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170,
CC ECO:0000269|PubMed:16330030};
CC KM=5.2 mM for D,L-glyceraldehyde (at 70 degrees Celsius and at pH 6)
CC {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170,
CC ECO:0000269|PubMed:16330030};
CC KM=7.1 mM for L-glyceraldehyde (at 70 degrees Celsius and at pH 6)
CC {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170,
CC ECO:0000269|PubMed:16330030};
CC KM=9.9 mM for KDGal (at 60 degrees Celsius and at pH 6)
CC {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170,
CC ECO:0000269|PubMed:16330030};
CC KM=25.7 mM for KDG (at 60 degrees Celsius and at pH 6)
CC {ECO:0000269|PubMed:10527934, ECO:0000269|PubMed:12824170,
CC ECO:0000269|PubMed:16330030};
CC Vmax=12.3 umol/min/mg enzyme with KDGal as substrate (at 60 degrees
CC Celsius and at pH 6) {ECO:0000269|PubMed:10527934,
CC ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030};
CC Vmax=15.7 umol/min/mg enzyme with pyruvate as substrate (at 70
CC degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934,
CC ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030};
CC Vmax=17.1 umol/min/mg enzyme with D,L-glyceraldehyde as substrate (at
CC 70 degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934,
CC ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030};
CC Vmax=18 umol/min/mg enzyme with D-glyceraldehyde as substrate (at 70
CC degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934,
CC ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030};
CC Vmax=18 umol/min/mg enzyme with L-glyceraldehyde as substrate (at 70
CC degrees Celsius and at pH 6) {ECO:0000269|PubMed:10527934,
CC ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030};
CC Vmax=51.4 umol/min/mg enzyme with KDG as substrate (at 60 degrees
CC Celsius and at pH 6) {ECO:0000269|PubMed:10527934,
CC ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030};
CC Note=kcat is 28.2 sec(-1) for KDG and 6.8 sec(-1) for KDGal.;
CC Temperature dependence:
CC Extremely thermostable. {ECO:0000269|PubMed:10527934,
CC ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16330030};
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:0000269|PubMed:10527934,
CC ECO:0000269|PubMed:15265860, ECO:0000269|Ref.5}.
CC -!- MISCELLANEOUS: The metabolic pathway in Sulfolobus species contrasts
CC with the situation observed in other microorganisms where separate
CC enzymes exist for the catabolism of the two sugars, glucose and
CC galactose. {ECO:0000305|PubMed:12824170}.
CC -!- SIMILARITY: Belongs to the DapA family. KDPG aldolase subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ224174; CAA11866.1; -; Genomic_DNA.
DR RefSeq; WP_009991687.1; NZ_LT549890.1.
DR PDB; 1W37; X-ray; 2.00 A; A/B/C/D=1-294.
DR PDB; 1W3I; X-ray; 1.70 A; A/B/C/D=2-294.
DR PDB; 1W3N; X-ray; 2.10 A; A/B/C/D=1-294.
DR PDB; 1W3T; X-ray; 2.10 A; A/B/C/D=1-294.
DR PDB; 2YDA; X-ray; 1.91 A; A/B=1-294.
DR PDB; 6G3Z; X-ray; 2.35 A; A/B=1-294.
DR PDB; 6GSO; X-ray; 2.00 A; A/B/C/D=2-294.
DR PDB; 6GT8; X-ray; 3.15 A; A/B=2-294.
DR PDB; 6GV2; X-ray; 2.10 A; A/B=1-294.
DR PDB; 6H2R; X-ray; 1.57 A; A/B/C/D=2-294.
DR PDB; 6H2S; X-ray; 2.17 A; A/B/C/D=2-294.
DR PDB; 6H7R; X-ray; 2.80 A; A/B/C/D=2-294.
DR PDB; 6H7S; X-ray; 3.20 A; A/B=2-294.
DR PDBsum; 1W37; -.
DR PDBsum; 1W3I; -.
DR PDBsum; 1W3N; -.
DR PDBsum; 1W3T; -.
DR PDBsum; 2YDA; -.
DR PDBsum; 6G3Z; -.
DR PDBsum; 6GSO; -.
DR PDBsum; 6GT8; -.
DR PDBsum; 6GV2; -.
DR PDBsum; 6H2R; -.
DR PDBsum; 6H2S; -.
DR PDBsum; 6H7R; -.
DR PDBsum; 6H7S; -.
DR AlphaFoldDB; O54288; -.
DR SMR; O54288; -.
DR PRIDE; O54288; -.
DR GeneID; 44128913; -.
DR KEGG; ag:CAA11866; -.
DR OMA; VVPPVCT; -.
DR OrthoDB; 65776at2157; -.
DR BioCyc; MetaCyc:MON-4861; -.
DR BRENDA; 4.1.2.14; 6163.
DR BRENDA; 4.1.2.55; 6163.
DR SABIO-RK; O54288; -.
DR UniPathway; UPA00856; UER00829.
DR EvolutionaryTrace; O54288; -.
DR GO; GO:0008674; F:2-dehydro-3-deoxy-6-phosphogalactonate aldolase activity; IDA:UniProtKB.
DR GO; GO:0008675; F:2-dehydro-3-deoxy-phosphogluconate aldolase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR PANTHER; PTHR12128; PTHR12128; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing; Lyase;
KW Schiff base.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10527934"
FT CHAIN 2..294
FT /note="2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-
FT deoxy-6-phosphogalactonate aldolase"
FT /id="PRO_0000422658"
FT ACT_SITE 155
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000269|PubMed:15265860"
FT BINDING 43..44
FT /ligand="substrate"
FT BINDING 130..132
FT /ligand="substrate"
FT BINDING 155..157
FT /ligand="substrate"
FT SITE 130
FT /note="Proton shuttle"
FT /evidence="ECO:0000250"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1W3I"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1W3I"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:1W3I"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1W3I"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:1W3I"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1W3I"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:1W3I"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1W3I"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:1W3I"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1W3I"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1W3I"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:1W3I"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:1W3I"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:1W3I"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:1W3I"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:1W3I"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:1W3I"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:1W3I"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:2YDA"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:1W3I"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:1W3I"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:1W3I"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:1W3I"
FT HELIX 219..237
FT /evidence="ECO:0007829|PDB:1W3I"
FT HELIX 241..253
FT /evidence="ECO:0007829|PDB:1W3I"
FT HELIX 269..288
FT /evidence="ECO:0007829|PDB:1W3I"
SQ SEQUENCE 294 AA; 33108 MW; D709A94ACF68B0EF CRC64;
MPEIITPIIT PFTKDNRIDK EKLKIHAENL IRKGIDKLFV NGTTGLGPSL SPEEKLENLK
AVYDVTNKII FQVGGLNLDD AIRLAKLSKD FDIVGIASYA PYYYPRMSEK HLVKYFKTLC
EVSPHPVYLY NYPTATGKDI DAKVAKEIGC FTGVKDTIEN IIHTLDYKRL NPNMLVYSGS
DMLIATVAST GLDGNVAAGS NYLPEVTVTI KKLAMERKID EALKLQFLHD EVIEASRIFG
SLSSNYVLTK YFQGYDLGYP RPPIFPLDDE EERQLIKKVE GIRAKLVELK ILKE
