ID   KDSA_PARP8              Reviewed;         284 AA.
AC   B2JIX1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   28-JAN-2026, entry version 80.
DE   RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000255|HAMAP-Rule:MF_00056};
DE            EC=2.5.1.55 {ECO:0000255|HAMAP-Rule:MF_00056};
DE   AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00056};
DE   AltName: Full=KDO-8-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00056};
DE            Short=KDO 8-P synthase {ECO:0000255|HAMAP-Rule:MF_00056};
DE            Short=KDOPS {ECO:0000255|HAMAP-Rule:MF_00056};
DE   AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase {ECO:0000255|HAMAP-Rule:MF_00056};
GN   Name=kdsA {ECO:0000255|HAMAP-Rule:MF_00056};
GN   OrderedLocusNames=Bphy_1440;
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA   James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA   Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA   Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT   range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
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:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_00056}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00056}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00056,
CC       ECO:0000255|PROSITE-ProRule:PRU01406}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family. KdsA
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01406}.
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DR   EMBL; CP001043; ACC70622.1; -; Genomic_DNA.
DR   RefSeq; WP_012400835.1; NC_010622.1.
DR   AlphaFoldDB; B2JIX1; -.
DR   SMR; B2JIX1; -.
DR   STRING; 391038.Bphy_1440; -.
DR   KEGG; bph:Bphy_1440; -.
DR   eggNOG; COG2877; Bacteria.
DR   HOGENOM; CLU_036666_0_0_4; -.
DR   OrthoDB; 9776934at2; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000001192; Chromosome 1.
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   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; PRK05198.1; 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; Lipopolysaccharide biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN           1..284
FT                   /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT                   /id="PRO_1000091803"
FT   DOMAIN          11..274
FT                   /note="DAHPS class-I TIM-barrel"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         21
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         50
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         55
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         133
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         169
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         201
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         238
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         249
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
SQ   SEQUENCE   284 AA;  30963 MW;  C5AA63A66A3FCD13 CRC64;
     MKLGDFEIGL DKPFFLIAGT CVVESEQMTI DTAGKLKEIC AKLKIPFIYK SSYDKANRSS
     GKSFRGLGMD EGLRILSEVK RQLGLHVLTD VHSEHEIEPV ASVVDVLQTP AFLCRQTDFI
     HACARSGKPV NIKKGQFLAP HDMKNVIDKA RDAAREAGLS EDRFMACERG VSFGYNNLVS
     DMRSLAIMRE TGAPVVFDAT HSVQLPGGQG TSSGGQREFV PVLARAAVAT GIAGLFMETH
     PNPAEAKSDG PNAVPLHRMA DLLETLMTLD QAVKRTPFLE NDFN
//