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Database: UniProt
Entry: KDSA_GEOSL
LinkDB: KDSA_GEOSL
Original site: KDSA_GEOSL 
ID   KDSA_GEOSL              Reviewed;         272 AA.
AC   P61655;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   08-MAY-2019, entry version 91.
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=GSU1894;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R.,
RA   Van Aken S.E., Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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; AE017180; AAR35270.1; -; Genomic_DNA.
DR   RefSeq; NP_952943.1; NC_002939.5.
DR   RefSeq; WP_010942539.1; NC_002939.5.
DR   SMR; P61655; -.
DR   STRING; 243231.GSU1894; -.
DR   EnsemblBacteria; AAR35270; AAR35270; GSU1894.
DR   GeneID; 2686233; -.
DR   KEGG; gsu:GSU1894; -.
DR   PATRIC; fig|243231.5.peg.1932; -.
DR   eggNOG; ENOG4105CXR; Bacteria.
DR   eggNOG; COG2877; LUCA.
DR   HOGENOM; HOG000023021; -.
DR   InParanoid; P61655; -.
DR   KO; K01627; -.
DR   OMA; FRGIPTM; -.
DR   BioCyc; GSUL243231:G1G0I-2114-MONOMER; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000000577; 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    272       2-dehydro-3-deoxyphosphooctonate
FT                                aldolase.
FT                                /FTId=PRO_0000187129.
SQ   SEQUENCE   272 AA;  29488 MW;  0E83228CDCAE9DF9 CRC64;
     MTREITIGSV KIGGDRPLVL IAGPCVIENE AATLRCAERL MTICNGVSVS LVFKASYDKA
     NRTSVTSFRG PGMQEGLRIL QKVKDSLGIP VISDIHSIEQ VKPAAEVLDI IQVPAFLCRQ
     TDLVVEVGRT NRVVNVKKGQ FMAPWDMENV VGKILSTGNE RIILTERGVT FGYNNLVSDM
     RSLPIMRRIG FPVVFDATHS VQLPGGQGGS SGGQREFVEY LSRAAVATGI DGIFMEVHED
     PEKALCDGPN SVKLDDLPAL LKKLKAIDAI VK
//
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