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Database: UniProt
Entry: A0A2T0X4J8_9BACT
LinkDB: A0A2T0X4J8_9BACT
Original site: A0A2T0X4J8_9BACT 
ID   A0A2T0X4J8_9BACT        Unreviewed;       273 AA.
AC   A0A2T0X4J8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=3-deoxy-8-phosphooctulonate synthase {ECO:0000256|ARBA:ARBA00012693};
DE            EC=2.5.1.55 {ECO:0000256|ARBA:ARBA00012693};
GN   ORFNames=DFO77_12341 {ECO:0000313|EMBL:RCW30216.1};
OS   Marinilabilia salmonicolor.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC   Marinilabilia.
OX   NCBI_TaxID=989 {ECO:0000313|EMBL:RCW30216.1, ECO:0000313|Proteomes:UP000252733};
RN   [1] {ECO:0000313|EMBL:RCW30216.1, ECO:0000313|Proteomes:UP000252733}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=160A {ECO:0000313|EMBL:RCW30216.1,
RC   ECO:0000313|Proteomes:UP000252733};
RA   Lamendella R.;
RT   "Freshwater and sediment microbial communities from various areas in North
RT   America, analyzing microbe dynamics in response to fracking.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001069};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004756}.
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|ARBA:ARBA00004845}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the KdsA family.
CC       {ECO:0000256|ARBA:ARBA00010499}.
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:RCW30216.1}.
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DR   EMBL; QPIZ01000023; RCW30216.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0X4J8; -.
DR   STRING; 1168289.GCA_000259075_01905; -.
DR   OrthoDB; 9776934at2; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000252733; 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; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006269; KDO8P_synthase.
DR   NCBIfam; TIGR01362; KDO8P_synth; 1.
DR   PANTHER; PTHR21057:SF2; 2-DEHYDRO-3-DEOXYPHOSPHOOCTONATE ALDOLASE 1-RELATED; 1.
DR   PANTHER; PTHR21057; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252733};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..265
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   273 AA;  29681 MW;  FA13AF382E492107 CRC64;
     MNIKEIPGIK HTDSGQFFLL AGPCAIESED MALKIAEKAV KITDNLKIPY VFKGSYRKAN
     RSRIDSFTGI GDEKALKILR KVSETFDIPT ITDFHSAAEA QMAAEYVDIL QVPAFLCRQT
     DILVAAAKTG KVVSIKKGQF LAPEAMIFAI DKVRDSGNNK VMVTDRGTTF GYQDLIVDYR
     GIPTMKKMDV PVVLDITHSL QQPNQSTGVT GGKPELIETI AKAGIAVGAD GLFLETHFDP
     ANAKSDGANM LHLDHLSALL EKLTAIRSVV KGF
//
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