ID   KDSA_SHEPC              Reviewed;         282 AA.
AC   A4Y3K6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Sputcn32_0809;
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 / ATCC BAA-453;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-2007) 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         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; CP000681; ABP74539.1; -; Genomic_DNA.
DR   RefSeq; WP_011790622.1; NC_009438.1.
DR   AlphaFoldDB; A4Y3K6; -.
DR   SMR; A4Y3K6; -.
DR   STRING; 319224.Sputcn32_0809; -.
DR   GeneID; 45041244; -.
DR   KEGG; spc:Sputcn32_0809; -.
DR   eggNOG; COG2877; Bacteria.
DR   HOGENOM; CLU_036666_0_0_6; -.
DR   OMA; FRGIPTM; -.
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..282
FT                   /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT                   /id="PRO_1000003350"
SQ   SEQUENCE   282 AA;  30953 MW;  C629C8618B936BEB CRC64;
     MSNKIINLGS IEIANDKPFV LFGGMNVLES RDLAMSIAET YAEVTQKLGI PYVFKASFDK
     ANRSSVNSYR GPGMEEGLKI FEEIKKTFNL PLITDVHETY QCAPVAEVVD IIQLPAFLAR
     QTDLVVAMAK TGAIINVKKP QFLAPHEMRH IITKFNEAGN DEIILCERGS CFGYNNLVVD
     MLGMDEMKQS GYPVIFDATH ALQRPGGRSD SAGGRRAQAT ELARSGMALG LAGLFIEAHP
     DPDNAKCDGP CALPLHQLEN YLKQMKAIDD LVKSFEPIDT SK