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Database: UniProt
Entry: B9L728_NAUPA
LinkDB: B9L728_NAUPA
Original site: B9L728_NAUPA 
ID   B9L728_NAUPA            Unreviewed;       261 AA.
AC   B9L728;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   16-OCT-2019, entry version 75.
DE   RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000256|HAMAP-Rule:MF_00056};
DE            EC=2.5.1.55 {ECO:0000256|HAMAP-Rule:MF_00056};
DE   AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE   AltName: Full=KDO-8-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE            Short=KDO 8-P synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE            Short=KDOPS {ECO:0000256|HAMAP-Rule:MF_00056};
DE   AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase {ECO:0000256|HAMAP-Rule:MF_00056};
GN   Name=kdsA {ECO:0000256|HAMAP-Rule:MF_00056,
GN   ECO:0000313|EMBL:ACM92835.1};
GN   OrderedLocusNames=NAMH_1800 {ECO:0000313|EMBL:ACM92835.1};
OS   Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales;
OC   Nautiliaceae; Nautilia.
OX   NCBI_TaxID=598659 {ECO:0000313|EMBL:ACM92835.1, ECO:0000313|Proteomes:UP000000448};
RN   [1] {ECO:0000313|EMBL:ACM92835.1, ECO:0000313|Proteomes:UP000000448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1463 / DSM 18972 / AmH
RC   {ECO:0000313|Proteomes:UP000000448};
RX   PubMed=19197347; DOI=10.1371/journal.pgen.1000362;
RA   Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y.,
RA   Lee C.K., Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.;
RT   "Adaptations to submarine hydrothermal environments exemplified by the
RT   genome of Nautilia profundicola.";
RL   PLoS Genet. 5:E1000362-E1000362(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-
CC         deoxy-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;
CC         EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056,
CC         ECO:0000256|SAAS:SAAS01123735};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00056,
CC       ECO:0000256|SAAS:SAAS00700395}.
CC   -!- PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate
CC       biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-
CC       phosphate: step 2/3. {ECO:0000256|HAMAP-Rule:MF_00056,
CC       ECO:0000256|SAAS:SAAS00700401}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00056,
CC       ECO:0000256|SAAS:SAAS00700398}.
CC   -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00056, ECO:0000256|SAAS:SAAS00700400}.
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DR   EMBL; CP001279; ACM92835.1; -; Genomic_DNA.
DR   RefSeq; WP_015901887.1; NC_012115.1.
DR   STRING; 598659.NAMH_1800; -.
DR   EnsemblBacteria; ACM92835; ACM92835; NAMH_1800.
DR   KEGG; nam:NAMH_1800; -.
DR   eggNOG; ENOG4105CXR; Bacteria.
DR   eggNOG; COG2877; LUCA.
DR   HOGENOM; HOG000023021; -.
DR   KO; K01627; -.
DR   OMA; FRGIPTM; -.
DR   OrthoDB; 687380at2; -.
DR   BioCyc; NPRO598659:G1GU9-1775-MONOMER; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000000448; 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   Complete proteome {ECO:0000313|Proteomes:UP000000448};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00056,
KW   ECO:0000256|SAAS:SAAS00700397};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00056,
KW   ECO:0000256|SAAS:SAAS00700406};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00056,
KW   ECO:0000256|SAAS:SAAS00080156, ECO:0000313|EMBL:ACM92835.1}.
FT   DOMAIN        1    254       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   261 AA;  29422 MW;  C763ED9E801DA729 CRC64;
     MILIAGPCVI ESREQIFKIA EYLKPYNEKY DFYFKASYDK ANRTSLNSYR GPGIDKGLEI
     LNEVKEKFGY KLLTDVHETW QVKKAAEVVD VLQIPAFLCR QTDLLVEAAK TDKVVNIKKG
     QFMNPADMKY SVLKVLQTRG CNEATYENSL KHKVWLTERG TTFGYGNLVV DMRSLYIMRE
     YAPVIFDATH AVQMPGGAGG KSSGKREYVP VLSRAAAAVG IDGFFFETHY NPDEALSDGP
     NMITPETLEK TLKEIDCINK C
//
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