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Database: UniProt
Entry: U2KZH9_9BACT
LinkDB: U2KZH9_9BACT
Original site: U2KZH9_9BACT 
ID   U2KZH9_9BACT            Unreviewed;       255 AA.
AC   U2KZH9;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   08-MAY-2019, entry version 28.
DE   RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000256|SAAS:SAAS00700405};
DE            EC=2.5.1.55 {ECO:0000256|SAAS:SAAS00700404};
GN   Name=kdsA {ECO:0000313|EMBL:ERK03872.1};
GN   ORFNames=HMPREF1218_0317 {ECO:0000313|EMBL:ERK03872.1};
OS   Prevotella pleuritidis F0068.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1081904 {ECO:0000313|EMBL:ERK03872.1, ECO:0000313|Proteomes:UP000016600};
RN   [1] {ECO:0000313|EMBL:ERK03872.1, ECO:0000313|Proteomes:UP000016600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0068 {ECO:0000313|EMBL:ERK03872.1,
RC   ECO:0000313|Proteomes:UP000016600};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M.,
RA   Haft D.H., Methe B., Sutton G., Nelson K.E.;
RL   Submitted (AUG-2013) 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:ERK03872.1}.
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DR   EMBL; AWET01000007; ERK03872.1; -; Genomic_DNA.
DR   RefSeq; WP_021582988.1; NZ_AWET01000007.1.
DR   EnsemblBacteria; ERK03872; ERK03872; HMPREF1218_0317.
DR   PATRIC; fig|1081904.3.peg.292; -.
DR   BioCyc; GCF_000468135-HMP:HMPREF1218_RS01385-MONOMER; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000016600; 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:UP000016600};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00700397};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|SAAS:SAAS00700406};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016600};
KW   Transferase {ECO:0000256|SAAS:SAAS00080156,
KW   ECO:0000313|EMBL:ERK03872.1}.
FT   DOMAIN        4    249       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   255 AA;  28197 MW;  310382F55D128719 CRC64;
     MPPIFIAGPC VIESQELLDT VAETLVRINK KLGTDIFFKS SFDKANRTSI RSFRGPGLDK
     GLQMLADVKS KYGLKLLTDI HESYQADPVG EVVDVIQIPA FLCRQTDLLV SAAKTGRIIN
     IKKAQFLSGR DMQYPVEKAK DAGAREIWLT ERGNSFGYNN LVVDFRNIPD MQEIVPTVIM
     DCTHSVQRPG AGNGTTSGDR RFVPAMALAA KAFGANGYFF EVHPDPDRGL SDGPNMLELK
     QLEALIMRVN EEMSE
//
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