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Database: UniProt
Entry: A0A1F3XVA3_9PROT
LinkDB: A0A1F3XVA3_9PROT
Original site: A0A1F3XVA3_9PROT 
ID   A0A1F3XVA3_9PROT        Unreviewed;       293 AA.
AC   A0A1F3XVA3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   11-DEC-2019, entry version 9.
DE   RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000256|SAAS:SAAS00700405};
DE            EC=2.5.1.55 {ECO:0000256|SAAS:SAAS00700404};
GN   ORFNames=A2603_14350 {ECO:0000313|EMBL:OFZ79272.1};
OS   Bdellovibrionales bacterium RIFOXYD1_FULL_55_31.
OC   Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales.
OX   NCBI_TaxID=1797404 {ECO:0000313|EMBL:OFZ79272.1, ECO:0000313|Proteomes:UP000178677};
RN   [1] {ECO:0000313|EMBL:OFZ79272.1, ECO:0000313|Proteomes:UP000178677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-
CC         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; EC=2.5.1.55;
CC         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-phosphate:
CC       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 EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OFZ79272.1}.
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DR   EMBL; MEQK01000191; OFZ79272.1; -; Genomic_DNA.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000178677; 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   Cytoplasm {ECO:0000256|SAAS:SAAS00700397};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|SAAS:SAAS00700406};
KW   Transferase {ECO:0000256|SAAS:SAAS00080156}.
FT   DOMAIN          14..276
FT                   /note="DAHP_synth_1"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   293 AA;  31880 MW;  99EB216C12F9FE51 CRC64;
     MAAGTPNSFS LRPMPLIAGP CVLEDEALAL EIASELKRQL SGLPVELYFK ASFDKANRTS
     IDGFRGPGLK EGLKILDHVR AKTGLPLLTD FHTPEQARPV AEVVECLQVP AFLCRQTDMI
     IAGAEAALEF GRKLNVKKGQ FLAPWDAKNI VEKAKAVQAK HQGKAPAADW IYLTERGTSF
     GYNTLVVDMI SFQSMRKLGV PVIYDATHSI QTPGAGPGGK STGGKREYLE TLARAAMAAG
     ADGLFMECHP RPREAKSDGP NAFYLEHVGA FVRQLLAIRE LVQKQPRLLP EES
//
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