KDGA_THETE
ID KDGA_THETE Reviewed; 306 AA.
AC Q704D1;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolase;
DE Short=KD(P)G aldolase {ECO:0000303|PubMed:15869466};
DE EC=4.1.2.14 {ECO:0000269|PubMed:15869466, ECO:0000269|PubMed:18186475};
DE EC=4.1.2.51 {ECO:0000269|PubMed:15869466, ECO:0000269|PubMed:18186475};
GN Name=kdgA;
OS Thermoproteus tenax.
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=2271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=15028704; DOI=10.1128/jb.186.7.2179-2194.2004;
RA Siebers B., Tjaden B., Michalke K., Doerr C., Ahmed H., Zaparty M.,
RA Gordon P., Sensen C.W., Zibat A., Klenk H.-P., Schuster S.C., Hensel R.;
RT "Reconstruction of the central carbohydrate metabolism of Thermoproteus
RT tenax using genomic and biochemical data.";
RL J. Bacteriol. 186:2179-2194(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=15869466; DOI=10.1042/bj20041711;
RA Ahmed H., Ettema T.J., Tjaden B., Geerling A.C., van der Oost J.,
RA Siebers B.;
RT "The semi-phosphorylative Entner-Doudoroff pathway in hyperthermophilic
RT archaea: a re-evaluation.";
RL Biochem. J. 390:529-540(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 21-306 IN COMPLEX WITH SUBSTRATE,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBSTRATE SPECIFICITY, AND
RP SUBUNIT.
RX PubMed=18186475; DOI=10.1002/prot.21890;
RA Pauluhn A., Ahmed H., Lorentzen E., Buchinger S., Schomburg D., Siebers B.,
RA Pohl E.;
RT "Crystal structure and stereochemical studies of KD(P)G aldolase from
RT Thermoproteus tenax.";
RL Proteins 72:35-43(2008).
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 not able to use 2-keto-3-deoxy-6-phosphogalactonate
CC (KDPGal) and 2-keto-3-deoxygalactonate (KDGal) as substrate.
CC {ECO:0000269|PubMed:15028704, ECO:0000269|PubMed:15869466,
CC ECO:0000269|PubMed:18186475}.
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:15869466, ECO:0000269|PubMed:18186475};
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:15869466, ECO:0000269|PubMed:18186475};
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:18186475}.
CC -!- SIMILARITY: Belongs to the DapA family. KDPG aldolase subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ621282; CAF18463.1; -; Genomic_DNA.
DR PDB; 2R91; X-ray; 2.00 A; A/B/C/D=21-306.
DR PDB; 2R94; X-ray; 2.20 A; A/B/C/D=21-306.
DR PDBsum; 2R91; -.
DR PDBsum; 2R94; -.
DR AlphaFoldDB; Q704D1; -.
DR SMR; Q704D1; -.
DR BRENDA; 4.1.2.14; 6329.
DR UniPathway; UPA00856; UER00829.
DR EvolutionaryTrace; Q704D1; -.
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: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; Lyase; Schiff base.
FT CHAIN 1..306
FT /note="2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-
FT phosphogluconate aldolase"
FT /id="PRO_0000422660"
FT ACT_SITE 173
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000269|PubMed:18186475"
FT BINDING 61..62
FT /ligand="substrate"
FT BINDING 148..150
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 173..175
FT /ligand="substrate"
FT SITE 148
FT /note="Proton shuttle"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:2R91"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:2R91"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2R91"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:2R91"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:2R91"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:2R91"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:2R91"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:2R91"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:2R91"
FT HELIX 127..140
FT /evidence="ECO:0007829|PDB:2R91"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:2R91"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:2R91"
FT HELIX 160..166
FT /evidence="ECO:0007829|PDB:2R91"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:2R91"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:2R91"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:2R91"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:2R91"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:2R91"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:2R91"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:2R91"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:2R91"
FT HELIX 237..257
FT /evidence="ECO:0007829|PDB:2R91"
FT HELIX 259..271
FT /evidence="ECO:0007829|PDB:2R91"
FT HELIX 287..296
FT /evidence="ECO:0007829|PDB:2R91"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:2R91"
SQ SEQUENCE 306 AA; 33287 MW; 8F895D811AD8EDB8 CRC64;
MSHPLIPFRA NFLRAPRVLS MEIVAPVITT FRGGRLDPEL FANHVKNITS KGVDVVFVAG
TTGLGPALSL QEKMELTDAA TSAARRVIVQ VASLNADEAI ALAKYAESRG AEAVASLPPY
YFPRLSERQI AKYFRDLCSA VSIPVFLYNY PAAVGRDVDA RAAKELGCIR GVKDTNESLA
HTLAYKRYLP QARVYNGSDS LVFASFAVRL DGVVASSANY LPELLAGIRD AVAAGDIERA
RSLQFLLDEI VESARHIGYA AAVYELVEIF QGYEAGEPRG PVYPLDPEEK AWLRAAVAKA
KSQLRL
