KDSA_SYNPW
ID KDSA_SYNPW Reviewed; 283 AA.
AC A5GI92;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=SynWH7803_0231;
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32051;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7803;
RG Genoscope;
RL Submitted (MAY-2006) 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; CT971583; CAK22657.1; -; Genomic_DNA.
DR RefSeq; WP_011932161.1; NC_009481.1.
DR AlphaFoldDB; A5GI92; -.
DR SMR; A5GI92; -.
DR STRING; 32051.SynWH7803_0231; -.
DR EnsemblBacteria; CAK22657; CAK22657; SynWH7803_0231.
DR KEGG; syx:SynWH7803_0231; -.
DR eggNOG; COG2877; Bacteria.
DR HOGENOM; CLU_036666_0_0_3; -.
DR OMA; YRNIPEW; -.
DR OrthoDB; 687380at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR Proteomes; UP000001566; 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; -; 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..283
FT /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT /id="PRO_0000304498"
SQ SEQUENCE 283 AA; 30122 MW; C8AEEFF3EEAADFB1 CRC64;
MAARQVSLGS ITFANDAPFV LIGGVNVLES QQFALDAAAV YADVCRRLSI PLVFKASFDK
ANRSSIHSFR GPGLSDGLAM LQAVKDTHGI PVITDVHTPE QAAPAAEVCD IIQLPAFLAR
QTDLVQAMAG TGAVINIKKP QFLSPSQMAN VVEKFRECGN EQLLICERGS NFGYDNLVVD
MLGFGVMKRC CDDLPLIFDV THALQCRDPG GAASGGRRSQ VLDLARAGMA VGLAGLFLEA
HPDPSQARCD GPSALPLHQL EPFLSQLKAV DDLVKSLPAL TIQ
