ID A0A1D8UTP8_9PROT Unreviewed; 274 AA.
AC A0A1D8UTP8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000256|HAMAP-Rule:MF_00056};
DE EC=2.5.1.55 {ECO:0000256|HAMAP-Rule:MF_00056};
DE AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE AltName: Full=KDO-8-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE Short=KDO 8-P synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE Short=KDOPS {ECO:0000256|HAMAP-Rule:MF_00056};
DE AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase {ECO:0000256|HAMAP-Rule:MF_00056};
GN Name=kdsA {ECO:0000256|HAMAP-Rule:MF_00056,
GN ECO:0000313|EMBL:GEL64755.1};
GN ORFNames=A0U89_06615 {ECO:0000313|EMBL:AOX16857.1}, KBA01_20410
GN {ECO:0000313|EMBL:GEL64755.1};
OS Kozakia baliensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Kozakia.
OX NCBI_TaxID=153496 {ECO:0000313|EMBL:AOX16857.1, ECO:0000313|Proteomes:UP000179145};
RN [1] {ECO:0000313|EMBL:AOX16857.1, ECO:0000313|Proteomes:UP000179145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14400 {ECO:0000313|EMBL:AOX16857.1,
RC ECO:0000313|Proteomes:UP000179145};
RX PubMed=27716345;
RA Brandt J.U., Jakob F., Behr J., Geissler A.J., Vogel R.F.;
RT "Dissection of exopolysaccharide biosynthesis in Kozakia baliensis.";
RL Microb. Cell Fact. 15:170-170(2016).
RN [2] {ECO:0000313|EMBL:AOX16857.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 14400 {ECO:0000313|EMBL:AOX16857.1};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:GEL64755.1, ECO:0000313|Proteomes:UP000321177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16664 {ECO:0000313|EMBL:GEL64755.1,
RC ECO:0000313|Proteomes:UP000321177};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Kozakia baliensis NBRC 16664.";
RL Submitted (JUL-2019) 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, ECO:0000256|HAMAP-
CC Rule:MF_00056};
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, ECO:0000256|HAMAP-
CC Rule:MF_00056}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00056}.
CC -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000256|ARBA:ARBA00010499,
CC ECO:0000256|HAMAP-Rule:MF_00056}.
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DR EMBL; CP014674; AOX16857.1; -; Genomic_DNA.
DR EMBL; BJVW01000009; GEL64755.1; -; Genomic_DNA.
DR RefSeq; WP_070402571.1; NZ_CP014674.1.
DR AlphaFoldDB; A0A1D8UTP8; -.
DR STRING; 153496.A0U89_06615; -.
DR KEGG; kba:A0U89_06615; -.
DR eggNOG; COG2877; Bacteria.
DR OrthoDB; 9776934at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR Proteomes; UP000179145; Chromosome.
DR Proteomes; UP000321177; 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-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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00056};
KW Lipopolysaccharide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00056};
KW Reference proteome {ECO:0000313|Proteomes:UP000179145};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00056}.
FT DOMAIN 10..260
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 274 AA; 29084 MW; 4436F831193CD76D CRC64;
MNDFRIGSLS VGNELPFTLI AGPCQIESRD HAQDIAAALH EICHDLGIGL IYKSSFDKAN
RTSIGSKRGV GMASGLEILA GIREKFGCPV LTDVHSPEQC KPAAESVDVL QIPAFLCRQT
DLLLAAGETG AAINVKKGQF LAPWDMANVA AKIASTGNER IMLCERGTSF GYNTLVNDMR
GLPIMAQTGY PVVYDATHSV QQPGGLGGAS GGQREFVPPL ARAALAIGVA ALFIETHEAP
DRAPSDGPTM VPLSEMRALL TRLRAFDRLA KQDA
//