KDSA_BURCJ
ID KDSA_BURCJ Reviewed; 284 AA.
AC B4EDA2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {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 {ECO:0000255|HAMAP-Rule:MF_00056};
DE AltName: Full=KDO-8-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00056};
DE Short=KDO 8-P synthase {ECO:0000255|HAMAP-Rule:MF_00056};
DE Short=KDOPS {ECO:0000255|HAMAP-Rule:MF_00056};
DE AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase {ECO:0000255|HAMAP-Rule:MF_00056};
GN Name=kdsA {ECO:0000255|HAMAP-Rule:MF_00056};
GN OrderedLocusNames=BceJ2315_21430; ORFNames=BCAL2180;
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX PubMed=18931103; DOI=10.1128/jb.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM747720; CAR52481.1; -; Genomic_DNA.
DR RefSeq; WP_006485302.1; NC_011000.1.
DR PDB; 3TML; X-ray; 1.90 A; A/B/C/D=1-284.
DR PDBsum; 3TML; -.
DR AlphaFoldDB; B4EDA2; -.
DR SMR; B4EDA2; -.
DR STRING; 216591.BCAL2180; -.
DR EnsemblBacteria; CAR52481; CAR52481; BCAL2180.
DR GeneID; 56558678; -.
DR KEGG; bcj:BCAL2180; -.
DR eggNOG; COG2877; Bacteria.
DR HOGENOM; CLU_036666_0_0_4; -.
DR OMA; FRGIPTM; -.
DR OrthoDB; 687380at2; -.
DR BioCyc; BCEN216591:G1G1V-2395-MON; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR Proteomes; UP000001035; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipopolysaccharide biosynthesis; Transferase.
FT CHAIN 1..284
FT /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT /id="PRO_1000091801"
FT STRAND 1..3
FT /evidence="ECO:0007829|PDB:3TML"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:3TML"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:3TML"
FT HELIX 26..43
FT /evidence="ECO:0007829|PDB:3TML"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:3TML"
FT HELIX 69..83
FT /evidence="ECO:0007829|PDB:3TML"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:3TML"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:3TML"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:3TML"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:3TML"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:3TML"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:3TML"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3TML"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:3TML"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:3TML"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:3TML"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:3TML"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:3TML"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3TML"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:3TML"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:3TML"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:3TML"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:3TML"
FT HELIX 219..230
FT /evidence="ECO:0007829|PDB:3TML"
FT STRAND 233..242
FT /evidence="ECO:0007829|PDB:3TML"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:3TML"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:3TML"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:3TML"
FT HELIX 259..274
FT /evidence="ECO:0007829|PDB:3TML"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:3TML"
SQ SEQUENCE 284 AA; 30948 MW; 8949DCBA73158BC8 CRC64;
MKLCDFEVGL DQPFFLIAGT CVVESEQMTI DTAGRLKEIC EKLNVPFIYK SSYDKANRSS
GKSFRGLGMD EGLRILSEVK RQLGLPVLTD VHSIDEIEQV ASVVDVLQTP AFLCRQTDFI
HACARSGKPV NIKKGQFLAP HDMKNVIDKA RDAAREAGLS EDRFMACERG VSFGYNNLVS
DMRSLAIMRE TNAPVVFDAT HSVQLPGGQG TSSGGQREFV PVLARAAVAT GVAGLFMETH
PNPAEAKSDG PNAVPLNRMG ALLETLVTLD QAVKRNPFLE NDFN
