ID C2M6H9_CAPGI Unreviewed; 262 AA.
AC C2M6H9;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=3-deoxy-8-phosphooctulonate synthase {ECO:0000256|ARBA:ARBA00012693};
DE EC=2.5.1.55 {ECO:0000256|ARBA:ARBA00012693};
GN Name=kdsA {ECO:0000313|EMBL:EEK14079.1};
GN ORFNames=CAPGI0001_0114 {ECO:0000313|EMBL:EEK14079.1};
OS Capnocytophaga gingivalis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=553178 {ECO:0000313|EMBL:EEK14079.1, ECO:0000313|Proteomes:UP000003622};
RN [1] {ECO:0000313|EMBL:EEK14079.1, ECO:0000313|Proteomes:UP000003622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33624 / DSM 3290 / CIP 102945 / JCM 12953 / NCTC 12372 /
RC 27 {ECO:0000313|Proteomes:UP000003622};
RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (APR-2009) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEK14079.1}.
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DR EMBL; ACLQ01000022; EEK14079.1; -; Genomic_DNA.
DR AlphaFoldDB; C2M6H9; -.
DR STRING; 553178.CAPGI0001_0114; -.
DR eggNOG; COG2877; Bacteria.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR Proteomes; UP000003622; Unassembled WGS sequence.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEK14079.1}.
FT DOMAIN 5..252
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 262 AA; 28834 MW; 1DD3E76B316E7F12 CRC64;
MKNSDNFFLL AGPCAIEGED MAMRIAEKIV KITTALDIPY TFKGSFKKAN RSRIDSFTGI
GDEKALKILQ KVSLTFGIPT ITDIHEIKDA EMAAEYVDVL QIPAFLVRQT DLVVAAAKTG
KKVNLKKGQF MSPESMKHAV QKVLDSGNDQ VWITDRGTMF GYQDMIVDFR GIPTMKQYAP
VVLDITHSLQ QPNQSSGVTG GRPDMIETIA RAGVVNNVDG IFVETHFDPA NAKSDGANML
HLDLLEGLLT RLVAIRKTIN TF
//
