KDSA_AQUAE
ID KDSA_AQUAE Reviewed; 267 AA.
AC O66496;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase;
DE EC=2.5.1.55;
DE AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase;
DE AltName: Full=KDO-8-phosphate synthase;
DE Short=KDO 8-P synthase;
DE Short=KDOPS;
DE AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase;
GN Name=kdsA; OrderedLocusNames=aq_085;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP CHARACTERIZATION.
RX PubMed=10491295; DOI=10.1006/bbrc.1999.1361;
RA Duewel H.S., Sheflyan G.Y., Woodard R.W.;
RT "Functional and biochemical characterization of a recombinant 3-deoxy-D-
RT manno-octulosonic acid 8-phosphate synthase from the hyperthermophilic
RT bacterium Aquifex aeolicus.";
RL Biochem. Biophys. Res. Commun. 263:346-351(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=12441100; DOI=10.1016/s0022-2836(02)01096-3;
RA Wang J., Duewel H.S., Stuckey J.A., Woodard R.W., Gatti D.L.;
RT "Function of His185 in Aquifex aeolicus 3-deoxy-D-manno-octulosonate 8-
RT phosphate synthase.";
RL J. Mol. Biol. 324:205-214(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-
CC alpha-D-manno-2-octulosonate-8-phosphate + phosphate;
CC Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;
CC -!- PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate
CC biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate:
CC step 2/3.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis.
CC -!- SUBUNIT: Oligomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000305}.
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DR EMBL; AE000657; AAC06457.1; -; Genomic_DNA.
DR PIR; E70308; E70308.
DR RefSeq; NP_213056.1; NC_000918.1.
DR RefSeq; WP_010879994.1; NC_000918.1.
DR PDB; 1FWN; X-ray; 1.94 A; A/B=1-267.
DR PDB; 1FWS; X-ray; 1.90 A; A/B=1-267.
DR PDB; 1FWT; X-ray; 1.90 A; A/B=1-267.
DR PDB; 1FWW; X-ray; 1.85 A; A/B=1-267.
DR PDB; 1FX6; X-ray; 2.06 A; A/B=1-267.
DR PDB; 1FXP; X-ray; 1.80 A; A/B=1-267.
DR PDB; 1FXQ; X-ray; 1.80 A; A/B=1-267.
DR PDB; 1FY6; X-ray; 1.89 A; A/B=1-267.
DR PDB; 1JCX; X-ray; 1.80 A; A/B=1-267.
DR PDB; 1JCY; X-ray; 1.90 A; A/B=1-267.
DR PDB; 1LRN; X-ray; 2.10 A; A/B=1-267.
DR PDB; 1LRO; X-ray; 1.80 A; A/B=1-267.
DR PDB; 1LRQ; X-ray; 1.80 A; A/B=1-267.
DR PDB; 1PCK; X-ray; 1.80 A; A/B=1-267.
DR PDB; 1PCW; X-ray; 1.85 A; A/B=1-267.
DR PDB; 1PE1; X-ray; 1.74 A; A/B=1-267.
DR PDB; 1T8X; X-ray; 1.80 A; A/B=1-267.
DR PDB; 1T96; X-ray; 1.85 A; A/B=1-267.
DR PDB; 1T99; X-ray; 1.85 A; A/B=1-267.
DR PDB; 1ZHA; X-ray; 1.74 A; A/B=1-267.
DR PDB; 1ZJI; X-ray; 2.25 A; A/B=1-267.
DR PDB; 2A21; X-ray; 1.80 A; A/B=1-267.
DR PDB; 2A2I; X-ray; 1.95 A; A/B=1-267.
DR PDB; 2EF9; X-ray; 2.00 A; A/B=1-267.
DR PDB; 2NWR; X-ray; 1.50 A; A/B=1-267.
DR PDB; 2NWS; X-ray; 1.80 A; A/B=1-267.
DR PDB; 2NX1; X-ray; 1.80 A; A/B=1-267.
DR PDB; 2NX3; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=1-267.
DR PDB; 2NXG; X-ray; 1.95 A; A/B=2-264.
DR PDB; 2NXH; X-ray; 2.11 A; A/B/C/D/E/F/G/H/I/J/K/L=2-264.
DR PDB; 2NXI; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L=2-264.
DR PDB; 3E0I; X-ray; 1.70 A; A/B=1-267.
DR PDB; 3E12; X-ray; 1.70 A; A/B=1-267.
DR PDBsum; 1FWN; -.
DR PDBsum; 1FWS; -.
DR PDBsum; 1FWT; -.
DR PDBsum; 1FWW; -.
DR PDBsum; 1FX6; -.
DR PDBsum; 1FXP; -.
DR PDBsum; 1FXQ; -.
DR PDBsum; 1FY6; -.
DR PDBsum; 1JCX; -.
DR PDBsum; 1JCY; -.
DR PDBsum; 1LRN; -.
DR PDBsum; 1LRO; -.
DR PDBsum; 1LRQ; -.
DR PDBsum; 1PCK; -.
DR PDBsum; 1PCW; -.
DR PDBsum; 1PE1; -.
DR PDBsum; 1T8X; -.
DR PDBsum; 1T96; -.
DR PDBsum; 1T99; -.
DR PDBsum; 1ZHA; -.
DR PDBsum; 1ZJI; -.
DR PDBsum; 2A21; -.
DR PDBsum; 2A2I; -.
DR PDBsum; 2EF9; -.
DR PDBsum; 2NWR; -.
DR PDBsum; 2NWS; -.
DR PDBsum; 2NX1; -.
DR PDBsum; 2NX3; -.
DR PDBsum; 2NXG; -.
DR PDBsum; 2NXH; -.
DR PDBsum; 2NXI; -.
DR PDBsum; 3E0I; -.
DR PDBsum; 3E12; -.
DR AlphaFoldDB; O66496; -.
DR SMR; O66496; -.
DR STRING; 224324.aq_085; -.
DR DrugBank; DB02992; 1-Deoxy-6-O-Phosphono-1-[(Phosphonomethyl)Amino]-L-Threo-Hexitol.
DR DrugBank; DB03248; 2-(Phosphonooxy)Butanoic Acid.
DR DrugBank; DB01709; 2-phospho-D-glyceric acid.
DR DrugBank; DB03745; Arabinose-5-phosphate.
DR DrugBank; DB03937; D-erythrose 4-phosphate.
DR DrugBank; DB01819; Phosphoenolpyruvate.
DR DrugBank; DB02053; Ribose-5-phosphate.
DR DrugBank; DB02433; {[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acid.
DR EnsemblBacteria; AAC06457; AAC06457; aq_085.
DR KEGG; aae:aq_085; -.
DR PATRIC; fig|224324.8.peg.75; -.
DR eggNOG; COG2877; Bacteria.
DR HOGENOM; CLU_036666_0_0_0; -.
DR InParanoid; O66496; -.
DR OMA; FRGIPTM; -.
DR OrthoDB; 687380at2; -.
DR BRENDA; 2.5.1.55; 396.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR EvolutionaryTrace; O66496; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008676; F:3-deoxy-8-phosphooctulonate synthase activity; IBA:GO_Central.
DR GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046364; P:monosaccharide biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00056; KDO8P_synth; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR006269; KDO8P_synthase.
DR PANTHER; PTHR21057; PTHR21057; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR TIGRFAMs; TIGR01362; KDO8P_synth; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipopolysaccharide biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..267
FT /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT /id="PRO_0000187099"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:2NWR"
FT HELIX 16..32
FT /evidence="ECO:0007829|PDB:2NWR"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2NWR"
FT HELIX 60..74
FT /evidence="ECO:0007829|PDB:2NWR"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:2NWR"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:2NWR"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:2NWR"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:2NWR"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2NWR"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:2NWR"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2NWR"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:2NWR"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:2NWR"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:2NWR"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:2NWR"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:2NWR"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:2NWR"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:2NWR"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:2NWR"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:2NWR"
FT TURN 190..193
FT /evidence="ECO:0007829|PDB:3E0I"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:3E0I"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:2NWR"
FT HELIX 204..214
FT /evidence="ECO:0007829|PDB:2NWR"
FT STRAND 217..225
FT /evidence="ECO:0007829|PDB:2NWR"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2NWR"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:3E12"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:2NWR"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1PE1"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:2NWR"
FT HELIX 243..258
FT /evidence="ECO:0007829|PDB:2NWR"
SQ SEQUENCE 267 AA; 29734 MW; 0A3CFEA3337F1964 CRC64;
MEKFLVIAGP CAIESEELLL KVGEEIKRLS EKFKEVEFVF KSSFDKANRS SIHSFRGHGL
EYGVKALRKV KEEFGLKITT DIHESWQAEP VAEVADIIQI PAFLCRQTDL LLAAAKTGRA
VNVKKGQFLA PWDTKNVVEK LKFGGAKEIY LTERGTTFGY NNLVVDFRSL PIMKQWAKVI
YDATHSVQLP GGLGDKSGGM REFIFPLIRA AVAVGCDGVF METHPEPEKA LSDASTQLPL
SQLEGIIEAI LEIREVASKY YETIPVK
