ID KDSA_PSEMY Reviewed; 281 AA. AC A4XWS2; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 82. 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=Pmen_3034; OS Pseudomonas mendocina (strain ymp). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=399739; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ymp; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Hersman L., Dubois J., Maurice P., Richardson P.; RT "Complete sequence of Pseudomonas mendocina ymp."; 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}. 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; CP000680; ABP85788.1; -; Genomic_DNA. DR AlphaFoldDB; A4XWS2; -. DR SMR; A4XWS2; -. DR STRING; 399739.Pmen_3034; -. DR KEGG; pmy:Pmen_3034; -. DR eggNOG; COG2877; Bacteria. DR HOGENOM; CLU_036666_0_0_6; -. DR OrthoDB; 9776934at2; -. 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; 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 PANTHER; PTHR21057:SF2; 2-DEHYDRO-3-DEOXYPHOSPHOOCTONATE ALDOLASE 1-RELATED; 1. DR PANTHER; PTHR21057; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1. DR Pfam; PF00793; DAHP_synth_1; 1. DR SUPFAM; SSF51569; Aldolase; 1. PE 3: Inferred from homology; KW Cytoplasm; Lipopolysaccharide biosynthesis; Transferase. FT CHAIN 1..281 FT /note="2-dehydro-3-deoxyphosphooctonate aldolase" FT /id="PRO_1000057397" SQ SEQUENCE 281 AA; 30833 MW; 3B224888594A12D3 CRC64; MAQKIIKVRD IEIANDKPFV LFGGINVLES RDLAMQACEE YVRVTEKLGI PYVFKASFDK ANRSSITSFR GPGLEEGMKI FEEVKKTFGV PVITDVHEPH QAAAVAEVCD IIQLPAFLSR QTDLVVAMAK TGAVINIKKA QFLAPQEMKH ILTKCEEAGN DQLILCERGS SFGYNNLVVD MLGFGIMKQF EYPVFFDVTH ALQMPGGRAD SAGGRRAQVT DLAKAGMSQG LAGLFLEAHP DPENAKCDGP CALRLNKLEP FLSQLKQLDD LVKSFPPIET A //