ID B3EPU3_CHLPB Unreviewed; 294 AA.
AC B3EPU3;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=3-deoxy-8-phosphooctulonate synthase {ECO:0000256|ARBA:ARBA00012693};
DE EC=2.5.1.55 {ECO:0000256|ARBA:ARBA00012693};
GN OrderedLocusNames=Cphamn1_2438 {ECO:0000313|EMBL:ACE05333.1};
OS Chlorobium phaeobacteroides (strain BS1).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=331678 {ECO:0000313|EMBL:ACE05333.1};
RN [1] {ECO:0000313|EMBL:ACE05333.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS1 {ECO:0000313|EMBL:ACE05333.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides BS1.";
RL Submitted (JUN-2008) 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}.
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DR EMBL; CP001101; ACE05333.1; -; Genomic_DNA.
DR AlphaFoldDB; B3EPU3; -.
DR STRING; 331678.Cphamn1_2438; -.
DR KEGG; cpb:Cphamn1_2438; -.
DR eggNOG; COG2877; Bacteria.
DR HOGENOM; CLU_036666_0_0_10; -.
DR OrthoDB; 9776934at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACE05333.1}.
FT DOMAIN 26..281
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 294 AA; 31984 MW; 01D9DCE57D31D8D6 CRC64;
MEVNIGLDSS VEKSQQFSVG NVKVPLDRGL FFIAGPCVIE GREMALDVAS VLHAIRESEG
IACIFKGSFR KANRSSAASF TGIGDSAALE ILGEIRGRFD MPVLTDVHET QEVERVSPYV
DVLQIPAFLS RQTDLLTAAG RSGLCVNIKK GQFMAPEDMA FAAQKVAETG NTRIMLTERG
TTFGYHNLVV DFRGIPEMSK TGYPVVYDAT HSLQLPSSAQ GTSGGVREYL LPMARAAVAA
GVHGLFFEVH PEPQHAMSDA ATQVSLKEFP EIVHQMQKLH ACIENQFFSS RSNF
//
