ID   KDSA_ACTPL              Reviewed;         286 AA.
AC   O68662;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 84.
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; Synonyms=cps5D;
OS   Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=715;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=J45;
RA   Ward C.K., Lawrence M.L., Inzana T.J.;
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF053723; AAC26633.1; -; Genomic_DNA.
DR   AlphaFoldDB; O68662; -.
DR   SMR; O68662; -.
DR   STRING; 228399.appser1_100; -.
DR   BRENDA; 2.5.1.55; 123.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
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..286
FT                   /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT                   /id="PRO_0000187097"
SQ   SEQUENCE   286 AA;  31343 MW;  AA0FF8ACF7B7E448 CRC64;
     MTILNKIVKV GNIEVANDKP FTLFGGMNVL ESRDMAMRVC EQYVEVTNKL GVPYVFKASF
     DKANRSSIHS YRGPGMEEGL KIFQELKDTF GVSIITDVHE IYQCKPVAEV VDIIQLPAFL
     ARQTDLVEAM ARTGVVINVK KPQFLSPGQM GNIVEKIAEC GNENVILCDR GTNFGYDNLV
     VDMLGFNIMK KVSKGCPVIF DVTHSLQCRD PFGAASGGRR DQVTELARSG MAIGLAGLFL
     EAHPDPNSAK CDGPSALPLS KLEAFVSQMK AIDDLVKSFE EIDTSR