KDSA_ECOLI
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 03-AUG-2022, entry version 132.
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; Proteobacteria; 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 SWISS-2DPAGE; P0A715; -.
DR jPOST; P0A715; -.
DR PaxDb; P0A715; -.
DR PRIDE; P0A715; -.
DR EnsemblBacteria; AAC74299; AAC74299; b1215.
DR EnsemblBacteria; BAA36073; BAA36073; BAA36073.
DR GeneID; 66674965; -.
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; FRGIPTM; -.
DR PhylomeDB; P0A715; -.
DR BioCyc; EcoCyc:KDO-8PSYNTH-MON; -.
DR BioCyc; MetaCyc:KDO-8PSYNTH-MON; -.
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 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; 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
