ID   KDSA_ECOLI              Reviewed;         284 AA.
AC   P0A715; P17579;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   27-MAR-2024, entry version 140.
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=b1215, JW1206;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=3039295; DOI=10.1007/bf00331603;
RA   Woisetschlaeger M., Hoegenauer G.;
RT   "The kdsA gene coding for 3-deoxy-D-manno-octulosonic acid 8-phosphate
RT   synthetase is part of an operon in Escherichia coli.";
RL   Mol. Gen. Genet. 207:369-373(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=7543480; DOI=10.1128/jb.177.15.4488-4500.1995;
RA   Strohmaier H., Remler P., Renner W., Hoegenauer G.;
RT   "Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic
RT   acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is
RT   growth phase regulated primarily at the transcriptional level in
RT   Escherichia coli K-12.";
RL   J. Bacteriol. 177:4488-4500(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   PROTEIN SEQUENCE OF 1-12.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded in the
RT   genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [7]
RP   CHARACTERIZATION, AND PROTEIN SEQUENCE OF 1-10.
RX   PubMed=7775423; DOI=10.1074/jbc.270.23.13698;
RA   Dotson G.D., Dua R.K., Clemens J.C., Wooten E.W., Woodard R.W.;
RT   "Overproduction and one-step purification of Escherichia coli 3-deoxy-D-
RT   manno-octulosonic acid 8-phosphate synthase and oxygen transfer studies
RT   during catalysis using isotopic-shifted heteronuclear NMR.";
RL   J. Biol. Chem. 270:13698-13705(1995).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=10926505; DOI=10.1006/jmbi.2000.3956;
RA   Wagner T., Kretsinger R.H., Bauerle R., Tolbert W.D.;
RT   "3-deoxy-D-manno-octulosonate-8-phosphate synthase from Escherichia coli.
RT   Model of binding of phosphoenolpyruvate and D-arabinose-5-phosphate.";
RL   J. Mol. Biol. 301:233-238(2000).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND MASS SPECTROMETRY.
RX   PubMed=11371194; DOI=10.1021/bi010339d;
RA   Asojo O., Friedman J., Adir N., Belakhov V., Shoham Y., Baasov T.;
RT   "Crystal structures of KDOP synthase in its binary complexes with the
RT   substrate phosphoenolpyruvate and with a mechanism-based inhibitor.";
RL   Biochemistry 40:6326-6334(2001).
CC   -!- FUNCTION: Synthesis of KDO 8-P which is required for lipid A maturation
CC       and cellular growth.
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: Homotrimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MASS SPECTROMETRY: Mass=30842; Mass_error=17; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11371194};
CC   -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000305}.
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DR   EMBL; X05552; CAA29067.1; -; Genomic_DNA.
DR   EMBL; U18555; AAC43441.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74299.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA36073.1; -; Genomic_DNA.
DR   PIR; I83573; SYECOL.
DR   RefSeq; NP_415733.1; NC_000913.3.
DR   RefSeq; WP_000811065.1; NZ_STEB01000023.1.
DR   PDB; 1D9E; X-ray; 2.40 A; A/B/C/D=1-284.
DR   PDB; 1G7U; X-ray; 2.80 A; A=1-284.
DR   PDB; 1G7V; X-ray; 2.40 A; A=1-284.
DR   PDB; 1GG0; X-ray; 3.00 A; A=1-284.
DR   PDB; 1PHQ; X-ray; 2.70 A; A=1-284.
DR   PDB; 1PHW; X-ray; 2.36 A; A=1-284.
DR   PDB; 1PL9; X-ray; 2.90 A; A=1-284.
DR   PDB; 1Q3N; X-ray; 2.70 A; A=1-284.
DR   PDB; 1X6U; X-ray; 2.70 A; A=1-284.
DR   PDB; 1X8F; X-ray; 2.40 A; A=1-284.
DR   PDB; 6U57; X-ray; 2.80 A; A=1-284.
DR   PDBsum; 1D9E; -.
DR   PDBsum; 1G7U; -.
DR   PDBsum; 1G7V; -.
DR   PDBsum; 1GG0; -.
DR   PDBsum; 1PHQ; -.
DR   PDBsum; 1PHW; -.
DR   PDBsum; 1PL9; -.
DR   PDBsum; 1Q3N; -.
DR   PDBsum; 1X6U; -.
DR   PDBsum; 1X8F; -.
DR   PDBsum; 6U57; -.
DR   AlphaFoldDB; P0A715; -.
DR   SMR; P0A715; -.
DR   BioGRID; 4260117; 448.
DR   DIP; DIP-35940N; -.
DR   IntAct; P0A715; 47.
DR   STRING; 511145.b1215; -.
DR   jPOST; P0A715; -.
DR   PaxDb; 511145-b1215; -.
DR   EnsemblBacteria; AAC74299; AAC74299; b1215.
DR   GeneID; 75203328; -.
DR   GeneID; 945785; -.
DR   KEGG; ecj:JW1206; -.
DR   KEGG; eco:b1215; -.
DR   PATRIC; fig|1411691.4.peg.1069; -.
DR   EchoBASE; EB0513; -.
DR   eggNOG; COG2877; Bacteria.
DR   HOGENOM; CLU_036666_0_0_6; -.
DR   InParanoid; P0A715; -.
DR   OMA; KGQFMSP; -.
DR   OrthoDB; 9776934at2; -.
DR   PhylomeDB; P0A715; -.
DR   BioCyc; EcoCyc:KDO-8PSYNTH-MONOMER; -.
DR   BioCyc; MetaCyc:KDO-8PSYNTH-MONOMER; -.
DR   BRENDA; 2.5.1.55; 2026.
DR   SABIO-RK; P0A715; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   EvolutionaryTrace; P0A715; -.
DR   PRO; PR:P0A715; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR   GO; GO:0008676; F:3-deoxy-8-phosphooctulonate synthase activity; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IDA:EcoCyc.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00056; KDO8P_synth; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006269; KDO8P_synthase.
DR   NCBIfam; TIGR01362; KDO8P_synth; 1.
DR   PANTHER; PTHR21057:SF2; 2-DEHYDRO-3-DEOXYPHOSPHOOCTONATE ALDOLASE 1-RELATED; 1.
DR   PANTHER; PTHR21057; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SWISS-2DPAGE; P0A715; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing;
KW   Lipopolysaccharide biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..284
FT                   /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT                   /id="PRO_0000187124"
FT   CONFLICT        22
FT                   /note="F -> L (in Ref. 1; CAA29067)"
FT                   /evidence="ECO:0000305"
FT   STRAND          6..8
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   STRAND          15..17
FT                   /evidence="ECO:0007829|PDB:1G7V"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   STRAND          24..27
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   HELIX           31..48
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   STRAND          55..58
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   STRAND          64..68
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   HELIX           74..88
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   TURN            99..101
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   HELIX           102..108
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   STRAND          110..114
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   HELIX           116..119
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   HELIX           122..131
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   STRAND          134..139
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   HELIX           145..147
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   HELIX           148..156
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   TURN            157..159
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   STRAND          163..167
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   STRAND          173..175
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   HELIX           183..190
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   TURN            191..193
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   STRAND          196..199
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   HELIX           201..204
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   STRAND          211..213
FT                   /evidence="ECO:0007829|PDB:1G7V"
FT   TURN            219..222
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   HELIX           223..231
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   STRAND          234..237
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   STRAND          240..242
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   HELIX           244..247
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   STRAND          250..252
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   HELIX           257..259
FT                   /evidence="ECO:0007829|PDB:1PHW"
FT   HELIX           260..275
FT                   /evidence="ECO:0007829|PDB:1PHW"
SQ   SEQUENCE   284 AA;  30833 MW;  35E79D692D134535 CRC64;
     MKQKVVSIGD INVANDLPFV LFGGMNVLES RDLAMRICEH YVTVTQKLGI PYVFKASFDK
     ANRSSIHSYR GPGLEEGMKI FQELKQTFGV KIITDVHEPS QAQPVADVVD VIQLPAFLAR
     QTDLVEAMAK TGAVINVKKP QFVSPGQMGN IVDKFKEGGN EKVILCDRGA NFGYDNLVVD
     MLGFSIMKKV SGNSPVIFDV THALQCRDPF GAASGGRRAQ VAELARAGMA VGLAGLFIEA
     HPDPEHAKCD GPSALPLAKL EPFLKQMKAI DDLVKGFEEL DTSK
//