ID C6X5R3_FLAB3 Unreviewed; 269 AA.
AC C6X5R3;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=3-deoxy-8-phosphooctulonate synthase {ECO:0000256|ARBA:ARBA00012693};
DE EC=2.5.1.55 {ECO:0000256|ARBA:ARBA00012693};
GN OrderedLocusNames=FIC_01303 {ECO:0000313|EMBL:ACU07751.1};
OS Flavobacteriaceae bacterium (strain 3519-10).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=531844 {ECO:0000313|EMBL:ACU07751.1, ECO:0000313|Proteomes:UP000001512};
RN [1] {ECO:0000313|EMBL:ACU07751.1, ECO:0000313|Proteomes:UP000001512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3519-10 {ECO:0000313|EMBL:ACU07751.1,
RC ECO:0000313|Proteomes:UP000001512};
RX PubMed=18622572; DOI=10.1007/s00792-008-0178-2;
RA Raymond J.A., Christner B.C., Schuster S.C.;
RT "A bacterial ice-binding protein from the Vostok ice core.";
RL Extremophiles 12:713-717(2008).
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; CP001673; ACU07751.1; -; Genomic_DNA.
DR AlphaFoldDB; C6X5R3; -.
DR STRING; 531844.FIC_01303; -.
DR KEGG; fba:FIC_01303; -.
DR eggNOG; COG2877; Bacteria.
DR HOGENOM; CLU_036666_0_0_10; -.
DR OrthoDB; 9776934at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR Proteomes; UP000001512; Chromosome.
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 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 {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000001512};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACU07751.1}.
FT DOMAIN 9..267
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 269 AA; 29693 MW; EA47C40C8ECC8636 CRC64;
MIQHLDNIHH KNSSNFFLIA GPCIIEGEDM ALRIAEKVLE ITNRYQIPYI FKGSFKKANR
SRVDSFTTIG EEKSLEILKK VGETFNIPTT TDIHENEHAA LAANYVDVLQ IPAFLVRQTD
LLIAAAKTGK CITLKKGQFL SPESMKFAVE KVTDSGNEKT AIIERGNSFG YTDLVVDFRG
IPTMRNYAPV ILDVTHSLQQ PNQNSGVTGG RPELIETIAK AGIAVGADGL FIETHPDPSC
ALSDGANMLR LDKLEDLLQK LTRVRQAIL
//
