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Database: UniProt
Entry: F3PJW3_9BACE
LinkDB: F3PJW3_9BACE
Original site: F3PJW3_9BACE 
ID   F3PJW3_9BACE            Unreviewed;       266 AA.
AC   F3PJW3;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   08-MAY-2019, entry version 42.
DE   RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000256|SAAS:SAAS00700405};
DE            EC=2.5.1.55 {ECO:0000256|SAAS:SAAS00700404};
GN   ORFNames=HMPREF9445_02442 {ECO:0000313|EMBL:EGF50848.1};
OS   Bacteroides clarus YIT 12056.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=762984 {ECO:0000313|EMBL:EGF50848.1, ECO:0000313|Proteomes:UP000010321};
RN   [1] {ECO:0000313|EMBL:EGF50848.1, ECO:0000313|Proteomes:UP000010321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 12056 {ECO:0000313|EMBL:EGF50848.1,
RC   ECO:0000313|Proteomes:UP000010321};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B.,
RA   Courtney L., Fronick C., Harrison M., Strong C., Farmer C.,
RA   Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C.,
RA   Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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|SAAS:SAAS01123735};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {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|SAAS:SAAS00700401}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00700398}.
CC   -!- SIMILARITY: Belongs to the KdsA family.
CC       {ECO:0000256|SAAS:SAAS00700400}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EGF50848.1}.
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DR   EMBL; AFBM01000028; EGF50848.1; -; Genomic_DNA.
DR   RefSeq; WP_009122528.1; NZ_GL882598.1.
DR   STRING; 762984.HMPREF9445_02442; -.
DR   EnsemblBacteria; EGF50848; EGF50848; HMPREF9445_02442.
DR   eggNOG; ENOG4105CXR; Bacteria.
DR   eggNOG; COG2877; LUCA.
DR   BioCyc; GCF_000195615-HMP:HMPREF9445_RS11185-MONOMER; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000010321; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008676; F:3-deoxy-8-phosphooctulonate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 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:UP000010321};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00700397};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|SAAS:SAAS00700406};
KW   Transferase {ECO:0000256|SAAS:SAAS00080156}.
SQ   SEQUENCE   266 AA;  28878 MW;  69AC73BD0D9A7003 CRC64;
     MIELKNNPAG NFFLLAGPCV IEGEDMAMRI AERVAAITEK LQIPYAFKGS YRKANRSRLD
     SFMGIGDEKA LKVLKKVHDT FGVPTVTDIH AAEEAAMAAE YVDILQIPAF LCRQTDLLVA
     AAKTGKVINI KKGQFLSPLA MRFAADKVVE AGNKNVMITE RGTTFGYQDL VVDYRGIPEM
     QTFGFPVILD VTHSLQQPNQ TSGVTGGMPQ LIETIAKAGI AVGADGLFIE THENPAVAKS
     DGANMLKLDL LEGLLTKLVR IREAIK
//
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