KDSA_CHLMU
ID KDSA_CHLMU Reviewed; 269 AA.
AC Q9PLS0;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase;
DE EC=2.5.1.55;
DE AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase;
DE AltName: Full=KDO-8-phosphate synthase;
DE Short=KDO 8-P synthase;
DE Short=KDOPS;
DE AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase;
GN Name=kdsA; OrderedLocusNames=TC_0025;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
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 -!- PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate
CC biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate:
CC step 2/3.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000305}.
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DR EMBL; AE002160; AAF38916.1; -; Genomic_DNA.
DR PIR; E81747; E81747.
DR RefSeq; WP_010229162.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PLS0; -.
DR SMR; Q9PLS0; -.
DR STRING; 243161.TC_0025; -.
DR EnsemblBacteria; AAF38916; AAF38916; TC_0025.
DR GeneID; 1245549; -.
DR KEGG; cmu:TC_0025; -.
DR eggNOG; COG2877; Bacteria.
DR HOGENOM; CLU_036666_0_0_0; -.
DR OMA; FRGIPTM; -.
DR OrthoDB; 687380at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR Proteomes; UP000000800; 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; -; 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; Lipopolysaccharide biosynthesis; Transferase.
FT CHAIN 1..269
FT /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT /id="PRO_0000187116"
SQ SEQUENCE 269 AA; 29701 MW; 4851638139CDC88C CRC64;
MFPNNKMLLI AGPCVIEDNS VFETARRLKE IVAPYSSSVH WIFKSSYDKA NRSSLQNYRG
PGLKLGLQTL AKIKETFDVE ILTDVHSPDE AREAAKVCDI IQVPAFLCRQ TDLLVTAGET
QAIVNIKKGQ FLSPWEMQGP IDKVLSTGNN KIILTERGCS FGYNNLVSDM RSIEVLRRFG
FPVIFDGTHS IQLPGALQSQ SGGQTEFIPV LTRSAIAAGV HGLFIETHPN PASALSDAAS
MLSLKDLERL LPSWVQLFTY IQEMDTVSI
