KDSA_NEIMB
ID KDSA_NEIMB Reviewed; 280 AA.
AC Q9JZ55;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 119.
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}; OrderedLocusNames=NMB1283;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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; AE002098; AAF41659.1; -; Genomic_DNA.
DR PIR; B81100; B81100.
DR RefSeq; NP_274303.1; NC_003112.2.
DR RefSeq; WP_002222386.1; NC_003112.2.
DR PDB; 2QKF; X-ray; 1.75 A; A/B/C/D=1-280.
DR PDB; 3FYO; X-ray; 1.90 A; A/B/C/D=1-280.
DR PDB; 3FYP; X-ray; 1.85 A; A/B/C/D=1-280.
DR PDB; 3QPY; X-ray; 1.95 A; A/B/C/D=1-280.
DR PDB; 3QPZ; X-ray; 1.75 A; A/B/C/D=1-280.
DR PDB; 3QQ0; X-ray; 1.90 A; A/B/C/D=1-280.
DR PDB; 3QQ1; X-ray; 2.70 A; A/B/C/D=1-280.
DR PDB; 3STC; X-ray; 1.91 A; A/B/C/D=1-280.
DR PDB; 3STE; X-ray; 2.05 A; A/B/C/D=1-280.
DR PDB; 3STF; X-ray; 1.90 A; A/B/C/D=1-280.
DR PDB; 3STG; X-ray; 2.20 A; A/B/C/D=1-280.
DR PDB; 4JTE; X-ray; 1.90 A; A/B/C/D=1-280.
DR PDB; 4JTF; X-ray; 1.80 A; A/B/C/D=1-280.
DR PDB; 4JTG; X-ray; 1.85 A; A/B/C/D=1-280.
DR PDB; 4JTH; X-ray; 2.00 A; A/B/C/D=1-280.
DR PDB; 4JTI; X-ray; 1.75 A; A/B/C/D=1-280.
DR PDB; 4JTJ; X-ray; 1.75 A; A/B/C/D=1-280.
DR PDB; 4JTK; X-ray; 1.86 A; A/B/C/D=1-280.
DR PDB; 4JTL; X-ray; 2.10 A; A/B/C/D=1-280.
DR PDBsum; 2QKF; -.
DR PDBsum; 3FYO; -.
DR PDBsum; 3FYP; -.
DR PDBsum; 3QPY; -.
DR PDBsum; 3QPZ; -.
DR PDBsum; 3QQ0; -.
DR PDBsum; 3QQ1; -.
DR PDBsum; 3STC; -.
DR PDBsum; 3STE; -.
DR PDBsum; 3STF; -.
DR PDBsum; 3STG; -.
DR PDBsum; 4JTE; -.
DR PDBsum; 4JTF; -.
DR PDBsum; 4JTG; -.
DR PDBsum; 4JTH; -.
DR PDBsum; 4JTI; -.
DR PDBsum; 4JTJ; -.
DR PDBsum; 4JTK; -.
DR PDBsum; 4JTL; -.
DR AlphaFoldDB; Q9JZ55; -.
DR SMR; Q9JZ55; -.
DR STRING; 122586.NMB1283; -.
DR BindingDB; Q9JZ55; -.
DR ChEMBL; CHEMBL1938218; -.
DR PaxDb; Q9JZ55; -.
DR EnsemblBacteria; AAF41659; AAF41659; NMB1283.
DR KEGG; nme:NMB1283; -.
DR PATRIC; fig|122586.8.peg.1608; -.
DR HOGENOM; CLU_036666_0_0_4; -.
DR OMA; IKKPQFM; -.
DR BRENDA; 2.5.1.55; 3593.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR EvolutionaryTrace; Q9JZ55; -.
DR PRO; PR:Q9JZ55; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008676; F:3-deoxy-8-phosphooctulonate synthase activity; IBA:GO_Central.
DR GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0046364; P:monosaccharide biosynthetic process; IBA:GO_Central.
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;
KW Reference proteome; Transferase.
FT CHAIN 1..280
FT /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT /id="PRO_0000187143"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2QKF"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:2QKF"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:2QKF"
FT HELIX 28..45
FT /evidence="ECO:0007829|PDB:2QKF"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:2QKF"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:2QKF"
FT HELIX 71..85
FT /evidence="ECO:0007829|PDB:2QKF"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:2QKF"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:2QKF"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:2QKF"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:2QKF"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2QKF"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:2QKF"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2QKF"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2QKF"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:2QKF"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:2QKF"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:4JTI"
FT HELIX 180..187
FT /evidence="ECO:0007829|PDB:2QKF"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:2QKF"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:2QKF"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:2QKF"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:4JTI"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:4JTF"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:4JTF"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:2QKF"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:2QKF"
FT TURN 243..246
FT /evidence="ECO:0007829|PDB:3STG"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:3STG"
FT HELIX 256..273
FT /evidence="ECO:0007829|PDB:2QKF"
SQ SEQUENCE 280 AA; 30483 MW; 7183B4CC6E3FEE28 CRC64;
MDIKINDITL GNNSPFVLFG GINVLESLDS TLQTCAHYVE VTRKLGIPYI FKASFDKANR
SSIHSYRGVG LEEGLKIFEK VKAEFGIPVI TDVHEPHQCQ PVAEVCDVIQ LPAFLARQTD
LVVAMAKTGN VVNIKKPQFL SPSQMKNIVE KFHEAGNGKL ILCERGSSFG YDNLVVDMLG
FGVMKQTCGN LPVIFDVTHS LQTRDAGSAA SGGRRAQALD LALAGMATRL AGLFLESHPD
PKLAKCDGPS ALPLHLLEDF LIRIKALDDL IKSQPILTIE
