ID   KDSA_CHLTR              Reviewed;         269 AA.
AC   P0CD74; O84662; P77849;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   25-MAY-2022, entry version 58.
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=CT_655;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000305}.
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DR   EMBL; AE001273; AAC68250.1; -; Genomic_DNA.
DR   PIR; A71487; A71487.
DR   RefSeq; NP_220174.1; NC_000117.1.
DR   RefSeq; WP_009872027.1; NC_000117.1.
DR   AlphaFoldDB; P0CD74; -.
DR   SMR; P0CD74; -.
DR   STRING; 813.O172_03600; -.
DR   EnsemblBacteria; AAC68250; AAC68250; CT_655.
DR   GeneID; 884439; -.
DR   KEGG; ctr:CT_655; -.
DR   PATRIC; fig|272561.5.peg.721; -.
DR   HOGENOM; CLU_036666_0_0_0; -.
DR   InParanoid; P0CD74; -.
DR   OMA; FRGIPTM; -.
DR   BRENDA; 2.5.1.55; 1315.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008676; F:3-deoxy-8-phosphooctulonate synthase activity; IBA:GO_Central.
DR   GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IEA:UniProtKB-UniRule.
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   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_0000187119"
SQ   SEQUENCE   269 AA;  29617 MW;  20E93FF246E2702B CRC64;
     MFPENKMLLI AGPCVIEDNS VFETARRLKE IVAPYASSVH WIFKSSYDKA NRSSVHNYRG
     PGLKLGLQTL AKIKEELDVE ILTDVHSPDE AREAAKVCDI IQVPAFLCRQ TDLLVTAGET
     QAIVNIKKGQ FLSPWEMQGP IDKVLSTGNN KIILTERGCS FGYNNLVSDM RSIEVLRRFG
     FPVVFDGTHS VQLPGALHSQ SGGQTEFIPV LTRSAIAAGV QGLFIETHPN PSSALSDAAS
     MLSLKDLERL LPAWVQLFTY IQEMDAVSV