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Database: UniProt
Entry: KDSA_AQUAE
LinkDB: KDSA_AQUAE
Original site: KDSA_AQUAE 
ID   KDSA_AQUAE              Reviewed;         267 AA.
AC   O66496;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   18-SEP-2019, entry version 125.
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=aq_085;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=10491295; DOI=10.1006/bbrc.1999.1361;
RA   Duewel H.S., Sheflyan G.Y., Woodard R.W.;
RT   "Functional and biochemical characterization of a recombinant 3-deoxy-
RT   D-manno-octulosonic acid 8-phosphate synthase from the
RT   hyperthermophilic bacterium Aquifex aeolicus.";
RL   Biochem. Biophys. Res. Commun. 263:346-351(1999).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   PubMed=12441100; DOI=10.1016/s0022-2836(02)01096-3;
RA   Wang J., Duewel H.S., Stuckey J.A., Woodard R.W., Gatti D.L.;
RT   "Function of His185 in Aquifex aeolicus 3-deoxy-D-manno-octulosonate
RT   8-phosphate synthase.";
RL   J. Mol. Biol. 324:205-214(2002).
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;
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.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis.
CC   -!- SUBUNIT: Oligomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000305}.
DR   EMBL; AE000657; AAC06457.1; -; Genomic_DNA.
DR   PIR; E70308; E70308.
DR   RefSeq; NP_213056.1; NC_000918.1.
DR   RefSeq; WP_010879994.1; NC_000918.1.
DR   PDB; 1FWN; X-ray; 1.94 A; A/B=1-267.
DR   PDB; 1FWS; X-ray; 1.90 A; A/B=1-267.
DR   PDB; 1FWT; X-ray; 1.90 A; A/B=1-267.
DR   PDB; 1FWW; X-ray; 1.85 A; A/B=1-267.
DR   PDB; 1FX6; X-ray; 2.06 A; A/B=1-267.
DR   PDB; 1FXP; X-ray; 1.80 A; A/B=1-267.
DR   PDB; 1FXQ; X-ray; 1.80 A; A/B=1-267.
DR   PDB; 1FY6; X-ray; 1.89 A; A/B=1-267.
DR   PDB; 1JCX; X-ray; 1.80 A; A/B=1-267.
DR   PDB; 1JCY; X-ray; 1.90 A; A/B=1-267.
DR   PDB; 1LRN; X-ray; 2.10 A; A/B=1-267.
DR   PDB; 1LRO; X-ray; 1.80 A; A/B=1-267.
DR   PDB; 1LRQ; X-ray; 1.80 A; A/B=1-267.
DR   PDB; 1PCK; X-ray; 1.80 A; A/B=1-267.
DR   PDB; 1PCW; X-ray; 1.85 A; A/B=1-267.
DR   PDB; 1PE1; X-ray; 1.74 A; A/B=1-267.
DR   PDB; 1T8X; X-ray; 1.80 A; A/B=1-267.
DR   PDB; 1T96; X-ray; 1.85 A; A/B=1-267.
DR   PDB; 1T99; X-ray; 1.85 A; A/B=1-267.
DR   PDB; 1ZHA; X-ray; 1.74 A; A/B=1-267.
DR   PDB; 1ZJI; X-ray; 2.25 A; A/B=1-267.
DR   PDB; 2A21; X-ray; 1.80 A; A/B=1-267.
DR   PDB; 2A2I; X-ray; 1.95 A; A/B=1-267.
DR   PDB; 2EF9; X-ray; 2.00 A; A/B=1-267.
DR   PDB; 2NWR; X-ray; 1.50 A; A/B=1-267.
DR   PDB; 2NWS; X-ray; 1.80 A; A/B=1-267.
DR   PDB; 2NX1; X-ray; 1.80 A; A/B=1-267.
DR   PDB; 2NX3; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=1-267.
DR   PDB; 2NXG; X-ray; 1.95 A; A/B=2-264.
DR   PDB; 2NXH; X-ray; 2.11 A; A/B/C/D/E/F/G/H/I/J/K/L=2-264.
DR   PDB; 2NXI; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L=2-264.
DR   PDB; 3E0I; X-ray; 1.70 A; A/B=1-267.
DR   PDB; 3E12; X-ray; 1.70 A; A/B=1-267.
DR   PDBsum; 1FWN; -.
DR   PDBsum; 1FWS; -.
DR   PDBsum; 1FWT; -.
DR   PDBsum; 1FWW; -.
DR   PDBsum; 1FX6; -.
DR   PDBsum; 1FXP; -.
DR   PDBsum; 1FXQ; -.
DR   PDBsum; 1FY6; -.
DR   PDBsum; 1JCX; -.
DR   PDBsum; 1JCY; -.
DR   PDBsum; 1LRN; -.
DR   PDBsum; 1LRO; -.
DR   PDBsum; 1LRQ; -.
DR   PDBsum; 1PCK; -.
DR   PDBsum; 1PCW; -.
DR   PDBsum; 1PE1; -.
DR   PDBsum; 1T8X; -.
DR   PDBsum; 1T96; -.
DR   PDBsum; 1T99; -.
DR   PDBsum; 1ZHA; -.
DR   PDBsum; 1ZJI; -.
DR   PDBsum; 2A21; -.
DR   PDBsum; 2A2I; -.
DR   PDBsum; 2EF9; -.
DR   PDBsum; 2NWR; -.
DR   PDBsum; 2NWS; -.
DR   PDBsum; 2NX1; -.
DR   PDBsum; 2NX3; -.
DR   PDBsum; 2NXG; -.
DR   PDBsum; 2NXH; -.
DR   PDBsum; 2NXI; -.
DR   PDBsum; 3E0I; -.
DR   PDBsum; 3E12; -.
DR   SMR; O66496; -.
DR   STRING; 224324.aq_085; -.
DR   DrugBank; DB02992; 1-Deoxy-6-O-Phosphono-1-[(Phosphonomethyl)Amino]-L-Threo-Hexitol.
DR   DrugBank; DB03248; 2-(Phosphonooxy)Butanoic Acid.
DR   DrugBank; DB01709; 2-phospho-D-glyceric acid.
DR   DrugBank; DB03745; Arabinose-5-phosphate.
DR   DrugBank; DB03937; Erythose-4-Phosphate.
DR   DrugBank; DB01819; Phosphoenolpyruvate.
DR   DrugBank; DB02053; Ribose-5-phosphate.
DR   DrugBank; DB02433; {[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acid.
DR   EnsemblBacteria; AAC06457; AAC06457; aq_085.
DR   GeneID; 1192509; -.
DR   KEGG; aae:aq_085; -.
DR   PATRIC; fig|224324.8.peg.75; -.
DR   eggNOG; ENOG4105CXR; Bacteria.
DR   eggNOG; COG2877; LUCA.
DR   HOGENOM; HOG000023021; -.
DR   InParanoid; O66496; -.
DR   KO; K01627; -.
DR   OMA; FRGIPTM; -.
DR   OrthoDB; 687380at2; -.
DR   BioCyc; AAEO224324:G1G15-71-MONOMER; -.
DR   BRENDA; 2.5.1.55; 396.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   EvolutionaryTrace; O66496; -.
DR   Proteomes; UP000000798; 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   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Cytoplasm;
KW   Lipopolysaccharide biosynthesis; Reference proteome; Transferase.
FT   CHAIN         1    267       2-dehydro-3-deoxyphosphooctonate
FT                                aldolase.
FT                                /FTId=PRO_0000187099.
FT   STRAND        4      9       {ECO:0000244|PDB:2NWR}.
FT   HELIX        16     32       {ECO:0000244|PDB:2NWR}.
FT   STRAND       36     41       {ECO:0000244|PDB:2NWR}.
FT   HELIX        60     74       {ECO:0000244|PDB:2NWR}.
FT   STRAND       77     81       {ECO:0000244|PDB:2NWR}.
FT   HELIX        85     87       {ECO:0000244|PDB:2NWR}.
FT   HELIX        88     92       {ECO:0000244|PDB:2NWR}.
FT   STRAND       96    100       {ECO:0000244|PDB:2NWR}.
FT   HELIX       102    104       {ECO:0000244|PDB:2NWR}.
FT   HELIX       108    115       {ECO:0000244|PDB:2NWR}.
FT   TURN        116    118       {ECO:0000244|PDB:2NWR}.
FT   STRAND      119    124       {ECO:0000244|PDB:2NWR}.
FT   HELIX       131    134       {ECO:0000244|PDB:2NWR}.
FT   HELIX       135    143       {ECO:0000244|PDB:2NWR}.
FT   STRAND      147    153       {ECO:0000244|PDB:2NWR}.
FT   STRAND      159    161       {ECO:0000244|PDB:2NWR}.
FT   HELIX       169    173       {ECO:0000244|PDB:2NWR}.
FT   TURN        174    176       {ECO:0000244|PDB:2NWR}.
FT   STRAND      177    182       {ECO:0000244|PDB:2NWR}.
FT   HELIX       185    187       {ECO:0000244|PDB:2NWR}.
FT   TURN        190    193       {ECO:0000244|PDB:3E0I}.
FT   STRAND      194    196       {ECO:0000244|PDB:3E0I}.
FT   HELIX       201    203       {ECO:0000244|PDB:2NWR}.
FT   HELIX       204    214       {ECO:0000244|PDB:2NWR}.
FT   STRAND      217    225       {ECO:0000244|PDB:2NWR}.
FT   HELIX       227    229       {ECO:0000244|PDB:2NWR}.
FT   STRAND      231    233       {ECO:0000244|PDB:3E12}.
FT   TURN        234    236       {ECO:0000244|PDB:2NWR}.
FT   STRAND      237    239       {ECO:0000244|PDB:1PE1}.
FT   HELIX       240    242       {ECO:0000244|PDB:2NWR}.
FT   HELIX       243    258       {ECO:0000244|PDB:2NWR}.
SQ   SEQUENCE   267 AA;  29734 MW;  0A3CFEA3337F1964 CRC64;
     MEKFLVIAGP CAIESEELLL KVGEEIKRLS EKFKEVEFVF KSSFDKANRS SIHSFRGHGL
     EYGVKALRKV KEEFGLKITT DIHESWQAEP VAEVADIIQI PAFLCRQTDL LLAAAKTGRA
     VNVKKGQFLA PWDTKNVVEK LKFGGAKEIY LTERGTTFGY NNLVVDFRSL PIMKQWAKVI
     YDATHSVQLP GGLGDKSGGM REFIFPLIRA AVAVGCDGVF METHPEPEKA LSDASTQLPL
     SQLEGIIEAI LEIREVASKY YETIPVK
//
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