ID Q492V6_BLOPB Unreviewed; 277 AA.
AC Q492V6;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=3-deoxy-8-phosphooctulonate synthase {ECO:0000256|ARBA:ARBA00012693};
DE EC=2.5.1.55 {ECO:0000256|ARBA:ARBA00012693};
GN Name=kdsA {ECO:0000313|EMBL:AAZ40986.1};
GN OrderedLocusNames=BPEN_361 {ECO:0000313|EMBL:AAZ40986.1};
OS Blochmannia pennsylvanicus (strain BPEN).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX NCBI_TaxID=291272 {ECO:0000313|EMBL:AAZ40986.1, ECO:0000313|Proteomes:UP000007794};
RN [1] {ECO:0000313|EMBL:AAZ40986.1, ECO:0000313|Proteomes:UP000007794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPEN {ECO:0000313|EMBL:AAZ40986.1,
RC ECO:0000313|Proteomes:UP000007794};
RX PubMed=16077009; DOI=10.1101/gr.3771305;
RA Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT evolutionary trends among bacterial mutualists of insects.";
RL Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ40986.1; -; Genomic_DNA.
DR RefSeq; WP_011282895.1; NC_007292.1.
DR AlphaFoldDB; Q492V6; -.
DR STRING; 291272.BPEN_361; -.
DR KEGG; bpn:BPEN_361; -.
DR eggNOG; COG2877; Bacteria.
DR HOGENOM; CLU_036666_0_0_6; -.
DR OrthoDB; 9776934at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR Proteomes; UP000007794; Chromosome.
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:UP000007794};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..275
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 277 AA; 30962 MW; 00ECD248CFC90514 CRC64;
MQQLIVNISD IKVSNNLPFV LFGGMNVLES RDITMKVCEH YAKITHKLNI PHIFKASFDK
ANRSSIDSYR GPGLEEGLRL FQELQEIFGV KLMTDVHEIY QVKTVSEVVD VLQIPAFLAR
QTDLIASIAQ TGMPINIKKP QYMSPTQIIH IVKKCRSFSN KNIILCERGT VFGYDNLVVD
MLGFNVMNHV SKGCPIIVDV THALQKRNPL SPISGGRNRQ IYDMARASTA VGIAGLFLEA
HPNPHRAKCD GSSALPLNQL ENFLTQIKSI DELVKSF
//
