ALKD_PSEPU
ID ALKD_PSEPU Reviewed; 226 AA.
AC P00885; Q9EV78;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=2-dehydro-3-deoxy-phosphogluconate aldolase;
DE EC=4.1.2.14;
DE AltName: Full=KDPG-aldolase;
DE AltName: Full=Phospho-2-dehydro-3-deoxygluconate aldolase;
DE AltName: Full=Phospho-2-keto-3-deoxygluconate aldolase;
GN Name=eda;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H;
RX PubMed=12393206; DOI=10.1111/j.1574-6968.2002.tb11375.x;
RA Petruschka L., Adolf K., Burchhardt G., Dernedde J., Jurgensen J.,
RA Herrmann H.;
RT "Analysis of the zwf-pgl-eda-operon in Pseudomonas putida strains H and
RT KT2440.";
RL FEMS Microbiol. Lett. 215:89-95(2002).
RN [2]
RP PROTEIN SEQUENCE OF 2-226.
RX PubMed=6988426; DOI=10.1016/s0021-9258(19)85716-2;
RA Suzuki N., Wood W.A.;
RT "Complete primary structure of 2-keto-3-deoxy-6-phosphogluconate
RT aldolase.";
RL J. Biol. Chem. 255:3427-3435(1980).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=7161801; DOI=10.1016/0022-2836(82)90536-8;
RA Mavridis I.M., Hatada M.H., Tulinsky A., Lebioda L.;
RT "Structure of 2-keto-3-deoxy-6-phosphogluconate aldolase at 2.8-A
RT resolution.";
RL J. Mol. Biol. 162:419-444(1982).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX PubMed=974067; DOI=10.1021/bi00665a010;
RA Mavridis I.M., Tulinsky A.;
RT "The folding and quaternary structure of trimeric 2-keto-3-deoxy-6-
RT phosphogluconic aldolase at 3.5-A resolution.";
RL Biochemistry 15:4410-4417(1976).
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 -!- SUBUNIT: Homotrimer.
CC -!- SIMILARITY: Belongs to the KHG/KDPG aldolase family. {ECO:0000305}.
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DR EMBL; AJ279003; CAC14910.1; -; Genomic_DNA.
DR PIR; A01105; ADPSGP.
DR PDB; 1MXS; X-ray; 2.20 A; A=2-226.
DR PDBsum; 1MXS; -.
DR AlphaFoldDB; P00885; -.
DR SMR; P00885; -.
DR STRING; 1240350.AMZE01000025_gene1661; -.
DR eggNOG; COG0800; Bacteria.
DR EvolutionaryTrace; P00885; -.
DR GO; GO:0008675; F:2-dehydro-3-deoxy-phosphogluconate aldolase activity; IEA:UniProtKB-EC.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lyase; Schiff base.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6988426"
FT CHAIN 2..226
FT /note="2-dehydro-3-deoxy-phosphogluconate aldolase"
FT /id="PRO_0000201035"
FT ACT_SITE 61
FT ACT_SITE 145
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10118,
FT ECO:0000269|PubMed:6988426"
FT CONFLICT 110
FT /note="E -> Q (in Ref. 1; CAC14910)"
FT /evidence="ECO:0000305"
FT CONFLICT 195..196
FT /note="TG -> GT (in Ref. 1; CAC14910)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="I -> M (in Ref. 1; CAC14910)"
FT /evidence="ECO:0000305"
FT HELIX 13..27
FT /evidence="ECO:0007829|PDB:1MXS"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1MXS"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1MXS"
FT HELIX 41..50
FT /evidence="ECO:0007829|PDB:1MXS"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:1MXS"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:1MXS"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1MXS"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:1MXS"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:1MXS"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:1MXS"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:1MXS"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1MXS"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:1MXS"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:1MXS"
FT HELIX 154..162
FT /evidence="ECO:0007829|PDB:1MXS"
FT TURN 163..167
FT /evidence="ECO:0007829|PDB:1MXS"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:1MXS"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:1MXS"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:1MXS"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:1MXS"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:1MXS"
FT HELIX 209..221
FT /evidence="ECO:0007829|PDB:1MXS"
SQ SEQUENCE 226 AA; 24069 MW; 081FE3492F7A1452 CRC64;
MTTLERPQPK LSMADKAARI DAICEKARIL PVITIAREED ILPLADALAA GGIRTLEVTL
RSQHGLKAIQ VLREQRPELC VGAGTVLDRS MFAAVEAAGA QFVVTPGITE DILEAGVDSE
IPLLPGISTP SEIMMGYALG YRRFKLFPAE ISGGVAAIKA FGGPFGDIRF CPTGGVNPAN
VRNYMALPNV MCVGTGWMLD SSWIKNGDWA RIEACSAEAI ALLDAN
