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Database: UniProt
Entry: B9KFN8_CAMLR
LinkDB: B9KFN8_CAMLR
Original site: B9KFN8_CAMLR 
ID   B9KFN8_CAMLR            Unreviewed;       267 AA.
AC   B9KFN8;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 2.
DT   27-MAR-2024, entry version 87.
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   ECO:0000313|EMBL:ACM63873.2};
GN   OrderedLocusNames=Cla_0539 {ECO:0000313|EMBL:ACM63873.2};
OS   Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=306263 {ECO:0000313|EMBL:ACM63873.2, ECO:0000313|Proteomes:UP000007727};
RN   [1] {ECO:0000313|EMBL:ACM63873.2, ECO:0000313|Proteomes:UP000007727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM2100 / D67 / ATCC BAA-1060
RC   {ECO:0000313|Proteomes:UP000007727};
RX   PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA   Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT   "The complete genome sequence and analysis of the human pathogen
RT   Campylobacter lari.";
RL   Foodborne Pathog. Dis. 5:371-386(2008).
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, ECO:0000256|HAMAP-
CC         Rule:MF_00056};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004756, ECO:0000256|HAMAP-
CC       Rule:MF_00056}.
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, ECO:0000256|HAMAP-
CC       Rule:MF_00056}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00056}.
CC   -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000256|ARBA:ARBA00010499,
CC       ECO:0000256|HAMAP-Rule:MF_00056}.
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DR   EMBL; CP000932; ACM63873.2; -; Genomic_DNA.
DR   RefSeq; WP_041570271.1; NC_012039.1.
DR   AlphaFoldDB; B9KFN8; -.
DR   STRING; 306263.Cla_0539; -.
DR   GeneID; 7411099; -.
DR   KEGG; cla:CLA_0539; -.
DR   eggNOG; COG2877; Bacteria.
DR   HOGENOM; CLU_036666_0_0_7; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000007727; Chromosome.
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; Aldolase class I; 1.
DR   HAMAP; MF_00056; KDO8P_synth; 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, ECO:0000256|HAMAP-Rule:MF_00056};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00056};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007727};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00056}.
FT   DOMAIN          2..260
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   267 AA;  29402 MW;  10FE8940702514A2 CRC64;
     MKKMILIAGP CVIENEELVF KVAQELECFL KDDRIDFYFK SSFDKANRTS INSFRGPGLE
     KGLEILQKVK DKFGMQILTD IHESSQASIA AEVVDVLQIP AFLCRQTDLL VAAAKTKAKI
     NVKKGQFLNP EDIKYSVAKI LQTRGVIEEG FEIAKENGVF VAERGSSFGY GNLVVDMRSL
     VIMRKYAPVI FDATHSVQMP GINGGSSGGK SEFVEPLARA AAAVGVDGFF FETHLDPCKA
     LCDGPNMLDI SRLKNCVDTL LKIQEII
//
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