KDSA_ACIBT
ID KDSA_ACIBT Reviewed; 285 AA.
AC A3M5Y2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 25-MAY-2022, entry version 88.
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=A1S_1899;
OS Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS KC755 / 5377).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=400667;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX PubMed=17344419; DOI=10.1101/gad.1510307;
RA Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA Gerstein M., Snyder M.;
RT "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT density pyrosequencing and transposon mutagenesis.";
RL Genes Dev. 21:601-614(2007).
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; CP000521; ABO12326.2; -; Genomic_DNA.
DR RefSeq; WP_000080538.1; NZ_CP053098.1.
DR AlphaFoldDB; A3M5Y2; -.
DR SMR; A3M5Y2; -.
DR GeneID; 60879310; -.
DR KEGG; acb:A1S_1899; -.
DR HOGENOM; CLU_036666_0_0_6; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
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; Transferase.
FT CHAIN 1..285
FT /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT /id="PRO_1000091793"
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
