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Entry: A0A1I1AZS1_9BACT
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ID   A0A1I1AZS1_9BACT        Unreviewed;       276 AA.
AC   A0A1I1AZS1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   11-DEC-2019, entry version 7.
DE   RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000256|HAMAP-Rule:MF_00056};
DE            EC=2.5.1.55 {ECO:0000256|HAMAP-Rule:MF_00056};
DE   AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE   AltName: Full=KDO-8-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE            Short=KDO 8-P synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE            Short=KDOPS {ECO:0000256|HAMAP-Rule:MF_00056};
DE   AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase {ECO:0000256|HAMAP-Rule:MF_00056};
GN   Name=kdsA {ECO:0000256|HAMAP-Rule:MF_00056};
GN   ORFNames=SAMN04489723_11063 {ECO:0000313|EMBL:SFB43609.1};
OS   Algoriphagus aquimarinus.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=237018 {ECO:0000313|EMBL:SFB43609.1, ECO:0000313|Proteomes:UP000198790};
RN   [1] {ECO:0000313|EMBL:SFB43609.1, ECO:0000313|Proteomes:UP000198790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23399 {ECO:0000313|EMBL:SFB43609.1,
RC   ECO:0000313|Proteomes:UP000198790};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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|HAMAP-Rule:MF_00056,
CC         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|HAMAP-Rule:MF_00056,
CC       ECO:0000256|SAAS:SAAS00700401}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00056,
CC       ECO:0000256|SAAS:SAAS00700398}.
CC   -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00056, ECO:0000256|SAAS:SAAS00700400}.
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DR   EMBL; FOKK01000010; SFB43609.1; -; Genomic_DNA.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000198790; 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-UniRule.
DR   GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00056; KDO8P_synth; 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|HAMAP-Rule:MF_00056, ECO:0000256|SAAS:SAAS00700397};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00056,
KW   ECO:0000256|SAAS:SAAS00700406};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198790};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00056,
KW   ECO:0000256|SAAS:SAAS00080156}.
FT   DOMAIN          6..261
FT                   /note="DAHP_synth_1"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   276 AA;  30213 MW;  F0B81E24F2E64958 CRC64;
     MRVTDSVILG EDKPVLFSGP CAVESYDICL EIGTKVKAWA EQHGFSYVFK ASFDKANRTS
     SGSFRSIGMD KSLEVLQRVG KALNVPLVTD IHESYQVKDV AEVVDVLQIP AFLCRQTDLL
     LAAGESGKAV KIKRGQFMAP EDMQYAVTKV RSTGNENVCL TERGFSLGYH NLVVDMRGLP
     IMRQFAPVVF DITHSVQQPG GQGGTSGGQR EFAPILARAA AATGIDGFFI ETHPDPSVAL
     SDGPNLIPLH KMGQFLEMLK EAWILGRKYQ DFDVNN
//
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