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Database: UniProt
Entry: KDSA_PSEF5
LinkDB: KDSA_PSEF5
Original site: KDSA_PSEF5 
ID   KDSA_PSEF5              Reviewed;         281 AA.
AC   Q4KHF7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   08-MAY-2019, entry version 80.
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=PFL_1195;
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A.,
RA   Rosovitz M.J., Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W.,
RA   Nelson W.C., Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A.,
RA   Pierson L.S. III, Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas
RT   fluorescens Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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: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-
CC       phosphate: 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}.
DR   EMBL; CP000076; AAY90482.1; -; Genomic_DNA.
DR   RefSeq; WP_011059542.1; NC_004129.6.
DR   SMR; Q4KHF7; -.
DR   STRING; 220664.PFL_1195; -.
DR   PRIDE; Q4KHF7; -.
DR   EnsemblBacteria; AAY90482; AAY90482; PFL_1195.
DR   GeneID; 29822883; -.
DR   KEGG; pfl:PFL_1195; -.
DR   PATRIC; fig|220664.5.peg.1227; -.
DR   eggNOG; ENOG4105CXR; Bacteria.
DR   eggNOG; COG2877; LUCA.
DR   HOGENOM; HOG000023021; -.
DR   KO; K01627; -.
DR   OMA; FRGIPTM; -.
DR   OrthoDB; 687380at2; -.
DR   BioCyc; PPRO220664:G1G4K-1223-MONOMER; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000008540; 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; Cytoplasm; Lipopolysaccharide biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN         1    281       2-dehydro-3-deoxyphosphooctonate
FT                                aldolase.
FT                                /FTId=PRO_0000304472.
SQ   SEQUENCE   281 AA;  30705 MW;  C5200DDC2701909C CRC64;
     MAQKIIRVGN IEIANDKPMV LFGGMNVLES RDMAMQVCEE YVRVTEKLGI PYVFKASFDK
     ANRSSVTSYR GPGLEEGMRI FEDVKQAFGV PIITDVHEPA QAAVVAEVCD IIQLPAFLSR
     QTDLVVAMAK TGAVINIKKA QFLAPQEMKH ILSKCEEAGN DQLILCERGS SFGYNNLVVD
     MLGFGIMKQF EYPVFFDVTH ALQMPGGRAD SAGGRRAQVT DLAKAGMSQS LAGLFLEAHP
     DPDNAKCDGP CALRLDKLEP FLAQLKALDE LVKSFPTVET A
//
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