ID   E0SCL0_DICD3            Unreviewed;       284 AA.
AC   E0SCL0;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   04-NOV-2026, entry version 79.
DE   RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000256|HAMAP-Rule:MF_00056};
DE            EC=2.5.1.55 {ECO:0000256|HAMAP-Rule:MF_00056};
DE   AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE   AltName: Full=KDO-8-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE            Short=KDO 8-P synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE            Short=KDOPS {ECO:0000256|HAMAP-Rule:MF_00056};
DE   AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase {ECO:0000256|HAMAP-Rule:MF_00056};
GN   Name=kdsA {ECO:0000256|HAMAP-Rule:MF_00056,
GN   ECO:0000313|EMBL:ADM98534.1};
GN   OrderedLocusNames=Dda3937_00038 {ECO:0000313|EMBL:ADM98534.1};
OS   Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=198628 {ECO:0000313|EMBL:ADM98534.1, ECO:0000313|Proteomes:UP000006859};
RN   [1] {ECO:0000313|EMBL:ADM98534.1, ECO:0000313|Proteomes:UP000006859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3937 {ECO:0000313|EMBL:ADM98534.1,
RC   ECO:0000313|Proteomes:UP000006859};
RX   PubMed=21217001; DOI=10.1128/JB.01513-10;
RA   Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA   Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA   Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA   Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA   Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA   Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA   Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA   Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA   Blattner F.R., Keen N.T., Perna N.T.;
RT   "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL   J. Bacteriol. 193:2076-2077(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-arabinose 5-phosphate + phosphoenolpyruvate + H2O = 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         Evidence={ECO:0000256|ARBA:ARBA00049112, ECO:0000256|HAMAP-
CC         Rule:MF_00056};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004756, ECO:0000256|HAMAP-
CC       Rule:MF_00056}.
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. {ECO:0000256|ARBA:ARBA00004845, ECO:0000256|HAMAP-
CC       Rule:MF_00056}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00056,
CC       ECO:0000256|PROSITE-ProRule:PRU01406}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family. KdsA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00056}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01406}.
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DR   EMBL; CP002038; ADM98534.1; -; Genomic_DNA.
DR   RefSeq; WP_013317987.1; NC_014500.1.
DR   AlphaFoldDB; E0SCL0; -.
DR   STRING; 198628.Dda3937_00038; -.
DR   KEGG; ddd:Dda3937_00038; -.
DR   PATRIC; fig|198628.6.peg.2312; -.
DR   eggNOG; COG2877; Bacteria.
DR   HOGENOM; CLU_036666_0_0_6; -.
DR   OMA; ACEHYVK; -.
DR   OrthoDB; 9776934at2; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000006859; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008676; F:3-deoxy-8-phosphooctulonate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   FunFam; 3.20.20.70:FF:000058; 2-dehydro-3-deoxyphosphooctonate aldolase; 1.
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   NCBIfam; NF003543; kdsA; 1.
DR   NCBIfam; NF009109; kdsA; 1.
DR   PANTHER; PTHR21057; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS52061; DAHPS_I; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00056};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985,
KW   ECO:0000256|HAMAP-Rule:MF_00056};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006859};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00056}.
FT   DOMAIN          16..275
FT                   /note="DAHPS class-I TIM-barrel"
FT                   /evidence="ECO:0000259|PROSITE:PS52061"
FT   BINDING         55
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
FT   BINDING         60
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
FT   BINDING         138
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
FT   BINDING         168
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
SQ   SEQUENCE   284 AA;  30898 MW;  44CCFEE22107CD1B CRC64;
     MNNKVVNIGD IPVANSLPFV LFGGMNVLES RDLAMRICEH YVTVTQKLGI PYVFKASFDK
     ANRSSIHSYR GPGLEAGMKI FQELKQTFGV KIITDVHEPQ QAQPVSEVVD VIQLPAFLAR
     QTDLVEAMAK TDAVINIKKP QFISPGQVGN IVDKFREGGN EQVILCDRGS NFGYDNLVVD
     MLGFNVMKQV SHGAPVIFDV THALQCRDPF GAASGGRRAQ VAELARAGMA VGIAGLFIEA
     HPEPNSAMCD GPSALPLTKL EPFLQQMKAI DELVKSFPEL DTSN
//