ID I0EK37_HELC0 Unreviewed; 271 AA.
AC I0EK37;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
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 OrderedLocusNames=HCW_00015 {ECO:0000313|EMBL:AFI03306.1};
OS Helicobacter cetorum (strain ATCC BAA-429 / MIT 00-7128).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=182217 {ECO:0000313|EMBL:AFI03306.1, ECO:0000313|Proteomes:UP000005010};
RN [1] {ECO:0000313|Proteomes:UP000005010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-429 / MIT 00-7128 {ECO:0000313|Proteomes:UP000005010};
RA Kersulyte D., Berg D.E.;
RT "Complete genome sequence of Helicobacter cetorum strain MIT 00-7128.";
RL Submitted (APR-2012) 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, ECO:0000256|HAMAP-
CC 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: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; CP003479; AFI03306.1; -; Genomic_DNA.
DR RefSeq; WP_014660182.1; NC_017737.1.
DR AlphaFoldDB; I0EK37; -.
DR STRING; 182217.HCW_00015; -.
DR KEGG; hce:HCW_00015; -.
DR PATRIC; fig|182217.3.peg.3; -.
DR eggNOG; COG2877; Bacteria.
DR HOGENOM; CLU_036666_0_0_7; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR Proteomes; UP000005010; 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; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00056}.
FT DOMAIN 6..261
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 271 AA; 29779 MW; 50D620C6505206D1 CRC64;
MKLVKPILIA GPCVIESQEN LHAIAQRLKP LAQNEQIDFY FKASFDKANR TSLESYRGPG
LKKGLEMLQA IKDEFGYQIL TDVHESHQVE EVAKVADILQ IPAFLCRQTD LIVEASKTNA
IVNIKKGQFM NPKDMQYSVL KALKTRDASI MQPSYESALA NGVWLCERGS SFGYGNLVVD
MRSLVIMREF APVIFDATHS VQMPGGANGK SSGDSSFAPI LGRAASAVGI DGLFAETHIE
PKNALSDGAN MLKIEQLENL VTDMLKIQSL F
//
