KDSA2_BURPS
ID KDSA2_BURPS Reviewed; 281 AA.
AC Q63RA1;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase 2 {ECO:0000255|HAMAP-Rule:MF_00056};
DE EC=2.5.1.55 {ECO:0000255|HAMAP-Rule:MF_00056};
DE AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase 2 {ECO:0000255|HAMAP-Rule:MF_00056};
DE AltName: Full=KDO-8-phosphate synthase 2 {ECO:0000255|HAMAP-Rule:MF_00056};
DE Short=KDO 8-P synthase 2 {ECO:0000255|HAMAP-Rule:MF_00056};
DE Short=KDOPS 2 {ECO:0000255|HAMAP-Rule:MF_00056};
DE AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase 2 {ECO:0000255|HAMAP-Rule:MF_00056};
GN Name=kdsA2 {ECO:0000255|HAMAP-Rule:MF_00056}; OrderedLocusNames=BPSL2772;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_00056}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00056}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00056}.
CC -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000255|HAMAP-
CC Rule:MF_00056}.
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DR EMBL; BX571965; CAH36781.1; -; Genomic_DNA.
DR RefSeq; WP_004532215.1; NZ_CP009538.1.
DR RefSeq; YP_109367.1; NC_006350.1.
DR AlphaFoldDB; Q63RA1; -.
DR SMR; Q63RA1; -.
DR STRING; 272560.BPSL2772; -.
DR EnsemblBacteria; CAH36781; CAH36781; BPSL2772.
DR GeneID; 56528425; -.
DR KEGG; bps:BPSL2772; -.
DR PATRIC; fig|272560.51.peg.2541; -.
DR eggNOG; COG2877; Bacteria.
DR OMA; IKKPQFM; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR Proteomes; UP000000605; Chromosome 1.
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; -; 1.
DR HAMAP; MF_00056; KDO8P_synth; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR006269; KDO8P_synthase.
DR PANTHER; PTHR21057; PTHR21057; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR TIGRFAMs; TIGR01362; KDO8P_synth; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lipopolysaccharide biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..281
FT /note="2-dehydro-3-deoxyphosphooctonate aldolase 2"
FT /id="PRO_0000187111"
SQ SEQUENCE 281 AA; 30213 MW; FACA5DC907F1E273 CRC64;
MNVAISPGVT AGNSLPFVLF GGINVLESLD FTLDVCGEYV AVTRKLGIPF VFKASFDKAN
RSSIHSYRGV GLDEGLKIFA EVKARFGVPV ITDVHEVEQA APVAEIADVL QVPAFLARQT
DLVVAIAKAG KPVNVKKPQF MSPTQLKHVV SKCGEVGNDR VMLCERGSSF GYDNLVVDML
GFRQMAETTG GCPVIFDVTH SLQCRDPLGD ASGGRRRQVL DLARAGIAVG IAGLFLEAHP
DPDRARCDGP SALPLHQLEG FLSQMKAIDD LVKRMPALEI R
