ID D5LSG8_9ESCH Unreviewed; 144 AA.
AC D5LSG8;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=3-deoxy-8-phosphooctulonate synthase {ECO:0000256|ARBA:ARBA00012693};
DE EC=2.5.1.55 {ECO:0000256|ARBA:ARBA00012693};
DE Flags: Fragment;
GN Name=kdsA {ECO:0000313|EMBL:ADF44922.1};
OS Escherichia sp. H605.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=754321 {ECO:0000313|EMBL:ADF44922.1};
RN [1] {ECO:0000313|EMBL:ADF44922.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H605 {ECO:0000313|EMBL:ADF44922.1};
RA Walk S.T., Alm E.W., Gordon D.M., Ram J.L., Toranzos G.A., Tiedje J.M.,
RA Whittam T.S.;
RT "Cryptic Lineages of the Genus Escherichia.";
RL Submitted (MAR-2010) 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:0000256|ARBA:ARBA00001069};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004756}.
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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the KdsA family.
CC {ECO:0000256|ARBA:ARBA00010499}.
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DR EMBL; GU968129; ADF44922.1; -; Genomic_DNA.
DR AlphaFoldDB; D5LSG8; -.
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-EC.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR006269; KDO8P_synthase.
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 {ECO:0000256|ARBA:ARBA00022490};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..140
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADF44922.1"
FT NON_TER 144
FT /evidence="ECO:0000313|EMBL:ADF44922.1"
SQ SEQUENCE 144 AA; 15938 MW; 2227F4ACCC2FFE16 CRC64;
NDLPFVLFGG MNVLESRDLA MRICEHYVTV TQKLGIPYVF KASFDKANRS SIHSYRGPGL
EEGMKIFQEL KQTFGVKIIT DVHEPSQAQP VADVVDVIQL PAFLARQTDL VEAMAKTGAV
INVKKPQFVS PGQMGNIVDK FKEG
//
