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KDSA_HELPJ
ID   KDSA_HELPJ              Reviewed;         276 AA.
AC   Q9ZN55;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase;
DE            EC=2.5.1.55;
DE   AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase;
DE   AltName: Full=KDO-8-phosphate synthase;
DE            Short=KDO 8-P synthase;
DE            Short=KDOPS;
DE   AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase;
GN   Name=kdsA; OrderedLocusNames=jhp_0003;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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   -!- PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate
CC       biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate:
CC       step 2/3.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000305}.
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DR   EMBL; AE001439; AAD05587.1; -; Genomic_DNA.
DR   PIR; E71985; E71985.
DR   RefSeq; WP_000858336.1; NC_000921.1.
DR   AlphaFoldDB; Q9ZN55; -.
DR   SMR; Q9ZN55; -.
DR   STRING; 85963.jhp_0003; -.
DR   EnsemblBacteria; AAD05587; AAD05587; jhp_0003.
DR   KEGG; hpj:jhp_0003; -.
DR   eggNOG; COG2877; Bacteria.
DR   OMA; FRGIPTM; -.
DR   BRENDA; 2.5.1.55; 2604.
DR   SABIO-RK; Q9ZN55; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000000804; 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; -; 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..276
FT                   /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT                   /id="PRO_0000187134"
SQ   SEQUENCE   276 AA;  30374 MW;  EFE7D879FD48D3B8 CRC64;
     MKTSNTKTPK PVLIAGPCVI ESLENLRSIA IKLQPLANNE RLDFYFKASF DKANRTSLES
     YRGPGLEKGL EMLQTIKDEF GYKILTDVHE SYQASVAAKV ADILQIPAFL CRQTDLIVEV
     SQTNAIVNIK KGQFMNPKDM QYSVLKALKT RDSSIQSPTY ETALKNGVWL CERGSSFGYG
     NLVVDMRSLK IMREFAPVIF DATHSVQMPG GANGKSSGDS SFPPILPRAA AAVGIDGLFA
     ETHIDPKNAL SDGANMLKPD ELEHLVTDML KIQNLF
 
 
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