ID   Q1MH37_RHIJ3            Unreviewed;       281 AA.
AC   Q1MH37;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   04-NOV-2026, entry version 120.
DE   RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000256|HAMAP-Rule:MF_00056};
DE            EC=2.5.1.55 {ECO:0000256|HAMAP-Rule:MF_00056};
DE   AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE   AltName: Full=KDO-8-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE            Short=KDO 8-P synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE            Short=KDOPS {ECO:0000256|HAMAP-Rule:MF_00056};
DE   AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase {ECO:0000256|HAMAP-Rule:MF_00056};
GN   Name=kdsA {ECO:0000256|HAMAP-Rule:MF_00056,
GN   ECO:0000313|EMBL:CAK07730.1};
GN   OrderedLocusNames=RL2238 {ECO:0000313|EMBL:CAK07730.1};
OS   Rhizobium johnstonii (strain DSM 114642 / LMG 32736 / 3841) (Rhizobium
OS   leguminosarum bv. viciae).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium;
OC   Rhizobium johnstonii.
OX   NCBI_TaxID=216596 {ECO:0000313|EMBL:CAK07730.1, ECO:0000313|Proteomes:UP000006575};
RN   [1] {ECO:0000313|EMBL:CAK07730.1, ECO:0000313|Proteomes:UP000006575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 114642 / LMG 32736 / 3841
RC   {ECO:0000313|Proteomes:UP000006575};
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach A.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
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         Evidence={ECO:0000256|ARBA:ARBA00049112, ECO:0000256|HAMAP-
CC         Rule:MF_00056};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004756, ECO:0000256|HAMAP-
CC       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:0000256|ARBA:ARBA00004845, ECO:0000256|HAMAP-
CC       Rule:MF_00056}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00056,
CC       ECO:0000256|PROSITE-ProRule:PRU01406}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family. KdsA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00056}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01406}.
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DR   EMBL; AM236080; CAK07730.1; -; Genomic_DNA.
DR   RefSeq; WP_011651828.1; NC_008380.1.
DR   AlphaFoldDB; Q1MH37; -.
DR   EnsemblBacteria; CAK07730; CAK07730; RL2238.
DR   GeneID; 303207240; -.
DR   KEGG; rle:RL2238; -.
DR   eggNOG; COG2877; Bacteria.
DR   HOGENOM; CLU_036666_0_0_5; -.
DR   OMA; AACIRAM; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000006575; 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; kdsA; 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00056};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00056};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006575};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00056}.
FT   DOMAIN          23..279
FT                   /note="DAHPS class-I TIM-barrel"
FT                   /evidence="ECO:0000259|PROSITE:PS52061"
FT   BINDING         33
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
FT   BINDING         62
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
FT   BINDING         67
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
FT   BINDING         145
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
FT   BINDING         175
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
FT   BINDING         207
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
FT   BINDING         244
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
FT   BINDING         255
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
SQ   SEQUENCE   281 AA;  29935 MW;  564A6EA8F30F3513 CRC64;
     MSTDTNSEVR IGEGQGQVTF SNAGRLSLIA GPCQMESRDH AFMVAGTLKE LCGKLGIGLV
     YKSSFDKANR TSLSAERGIG IEKGMEVFAD LKKEFGFPVL TDVHTAEQCE EVAKVVDVLQ
     IPAFLCRQTD LLIAAAKTGR VVNVKKGQFL APWDMKNVLK KLNASGNPNV LLCERGASFG
     YNTLVSDMRS LPIMAAMGAP VVFDATHSVA QPGGQGESSG GQREFVETLA RAAVAAGIAG
     VFVETHQDPD NAPSDGPNMV YLKDMPRLLE KLLAFDAVAK A
//