ID   KDSA_CHLT2              Reviewed;         269 AA.
AC   B0B8N1; O84662; P77849;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
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}; OrderedLocusNames=CTL0024;
OS   Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=471472;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9119498; DOI=10.1128/iai.65.4.1527-1530.1997;
RA   Wylie J.L., Iliffe E.R., Wang L.L., McClarty G.;
RT   "Identification, characterization, and developmental regulation of
RT   Chlamydia trachomatis 3-deoxy-D-manno-octulosonate (KDO)-8-phosphate
RT   synthetase and CMP-KDO synthetase.";
RL   Infect. Immun. 65:1527-1530(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=434/Bu / ATCC VR-902B;
RX   PubMed=18032721; DOI=10.1101/gr.7020108;
RA   Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA   Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA   Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT   "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT   venereum isolates.";
RL   Genome Res. 18:161-171(2008).
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         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   -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00056}.
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DR   EMBL; U72493; AAB17556.1; -; Genomic_DNA.
DR   EMBL; AM884176; CAP03468.1; -; Genomic_DNA.
DR   RefSeq; WP_009873271.1; NC_010287.1.
DR   RefSeq; YP_001654115.1; NC_010287.1.
DR   AlphaFoldDB; B0B8N1; -.
DR   SMR; B0B8N1; -.
DR   EnsemblBacteria; CAP03468; CAP03468; CTL0024.
DR   KEGG; ctb:CTL0024; -.
DR   PATRIC; fig|471472.4.peg.27; -.
DR   HOGENOM; CLU_036666_0_0_0; -.
DR   OMA; FRGIPTM; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000000795; 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; -; 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   3: Inferred from homology;
KW   Cytoplasm; Lipopolysaccharide biosynthesis; Transferase.
FT   CHAIN           1..269
FT                   /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT                   /id="PRO_1000091804"
FT   CONFLICT        33
FT                   /note="A -> G (in Ref. 1; AAB17556)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        185
FT                   /note="F -> S (in Ref. 1; AAB17556)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225
FT                   /note="I -> K (in Ref. 1; AAB17556)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   269 AA;  29645 MW;  EE0B823CA45815EB CRC64;
     MFPENKMLLI AGPCVIEDNS VFETARRLKE IVAPYASSVH WIFKSSYDKA NRSSVHNYRG
     PGLRLGLQTL AKIKEELDVE ILTDVHSPDE AREAAKVCDI IQVPAFLCRQ TDLLVTAGET
     QAIVNIKKGQ FLSPWEMQGP IDKVLSTGNN KIILTERGCS FGYNNLVSDM RSIEVLRRFG
     FPVVFDGTHS VQLPGALHSQ SGGQTEFIPV LTRSAIAAGV QGLFIETHPN PSSALSDAAS
     MLSLKDLERL LPAWVQLFTY IQEMDAVSV