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Database: UniProt
Entry: A0A0S8K1V8_9BACE
LinkDB: A0A0S8K1V8_9BACE
Original site: A0A0S8K1V8_9BACE 
ID   A0A0S8K1V8_9BACE        Unreviewed;       271 AA.
AC   A0A0S8K1V8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   08-MAY-2019, entry version 13.
DE   RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000256|SAAS:SAAS00700405};
DE            EC=2.5.1.55 {ECO:0000256|SAAS:SAAS00700404};
GN   ORFNames=AMS26_06385 {ECO:0000313|EMBL:KPL15911.1};
OS   Bacteroides sp. SM23_62.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1703352 {ECO:0000313|EMBL:KPL15911.1, ECO:0000313|Proteomes:UP000050819};
RN   [1] {ECO:0000313|EMBL:KPL15911.1, ECO:0000313|Proteomes:UP000050819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_62 {ECO:0000313|EMBL:KPL15911.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur
RT   cycling among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPL15911.1}.
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DR   EMBL; LJUP01000041; KPL15911.1; -; Genomic_DNA.
DR   PATRIC; fig|1703352.3.peg.2459; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000050819; 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:UP000050819};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00700397};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|SAAS:SAAS00700406};
KW   Transferase {ECO:0000256|SAAS:SAAS00080156}.
FT   DOMAIN        9    268       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   271 AA;  29600 MW;  B709FA31ED8D8CA0 CRC64;
     MAGSVKVGNL EIGGGNPLVL FAGPCVLESE RIAFQTAERV KELAQKHNIP YIFKSSYLKA
     NRLSINSFVG PGLDKGLKIL RKLKKELDLT ILTDVHNPIE AEPVSQVADL LQIPAFLCRQ
     TDLVLSCART KKPLNIKKGQ FMAPEDMKKI AEKAESVGNK NILLTERGTS FGYHNLVVDM
     RSLVIMRDLG YPVIFDATHS LQLPGGESES SGGQPQFIIP LAKAAVACGC DGLFVETHPE
     ISSALSDKKS MLPLEEMEGF LVQIKKIEKA Q
//
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