ID KDSA_ACIB3 Reviewed; 285 AA.
AC B7H226;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
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=ABBFA_001556;
OS Acinetobacter baumannii (strain AB307-0294).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=557600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB307-0294;
RX PubMed=18931120; DOI=10.1128/jb.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT baumannii.";
RL J. Bacteriol. 190:8053-8064(2008).
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; CP001172; ACJ58772.1; -; Genomic_DNA.
DR RefSeq; WP_000080538.1; NZ_CP001172.1.
DR PDB; 6BNG; X-ray; 2.20 A; A/B=5-285.
DR PDBsum; 6BNG; -.
DR AlphaFoldDB; B7H226; -.
DR SMR; B7H226; -.
DR GeneID; 60879310; -.
DR HOGENOM; CLU_036666_0_0_6; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR Proteomes; UP000006924; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipopolysaccharide biosynthesis; Transferase.
FT CHAIN 1..285
FT /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT /id="PRO_1000116872"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:6BNG"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:6BNG"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:6BNG"
FT HELIX 35..52
FT /evidence="ECO:0007829|PDB:6BNG"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:6BNG"
FT HELIX 78..92
FT /evidence="ECO:0007829|PDB:6BNG"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:6BNG"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:6BNG"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:6BNG"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:6BNG"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:6BNG"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:6BNG"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:6BNG"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:6BNG"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:6BNG"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:6BNG"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:6BNG"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:6BNG"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:6BNG"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:6BNG"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:6BNG"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:6BNG"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:6BNG"
FT STRAND 236..245
FT /evidence="ECO:0007829|PDB:6BNG"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:6BNG"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:6BNG"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:6BNG"
FT HELIX 262..277
FT /evidence="ECO:0007829|PDB:6BNG"
SQ SEQUENCE 285 AA; 31550 MW; 8A66BA33FB4865BA CRC64;
MSQLKPQEVV RLGDIQMANH LPFVLFGGMN VLESKDLAFE IAETYIDICK RLDIPYVFKA
SFDKANRSSL HSFRGPGLEK GIEWLGDIKK HFNVPIITDV HEPYQAAPVA EVADIIQLPA
FLSRQTDLVE AMAKTQAIIN IKKAQFLAPH EMRHILHKCL EAGNDKLILC ERGSAFGYNN
LVVDMLGFDI MKEMNVPVFF DVTHALQTPG GRSDSAGGRR AQITTLARAG MATGLAGLFL
ESHPDPDKAK CDGPSALRLS QLEPFLAQLK ELDTLVKGFK KLDTH
//
