ID   KDSA_CHLMU              Reviewed;         269 AA.
AC   Q9PLS0;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   28-JAN-2026, entry version 125.
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=TC_0025;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
OC   Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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   -!- 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   -!- SUBCELLULAR LOCATION: Cytoplasm {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; AE002160; AAF38916.1; -; Genomic_DNA.
DR   PIR; E81747; E81747.
DR   RefSeq; WP_010229162.1; NC_002620.2.
DR   AlphaFoldDB; Q9PLS0; -.
DR   SMR; Q9PLS0; -.
DR   GeneID; 1245549; -.
DR   KEGG; cmu:TC_0025; -.
DR   eggNOG; COG2877; Bacteria.
DR   HOGENOM; CLU_036666_0_0_0; -.
DR   OrthoDB; 9780456at2; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000000800; 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   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..269
FT                   /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT                   /id="PRO_0000187116"
FT   DOMAIN          4..262
FT                   /note="DAHPS class-I TIM-barrel"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         14
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         44
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         49
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         127
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         157
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         189
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         226
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         237
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
SQ   SEQUENCE   269 AA;  29701 MW;  4851638139CDC88C CRC64;
     MFPNNKMLLI AGPCVIEDNS VFETARRLKE IVAPYSSSVH WIFKSSYDKA NRSSLQNYRG
     PGLKLGLQTL AKIKETFDVE ILTDVHSPDE AREAAKVCDI IQVPAFLCRQ TDLLVTAGET
     QAIVNIKKGQ FLSPWEMQGP IDKVLSTGNN KIILTERGCS FGYNNLVSDM RSIEVLRRFG
     FPVIFDGTHS IQLPGALQSQ SGGQTEFIPV LTRSAIAAGV HGLFIETHPN PASALSDAAS
     MLSLKDLERL LPSWVQLFTY IQEMDTVSI
//