KDSA_LEGPH
ID KDSA_LEGPH Reviewed; 274 AA.
AC Q5ZWA3;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000255|HAMAP-Rule:MF_00056};
DE EC=2.5.1.55 {ECO:0000255|HAMAP-Rule:MF_00056};
DE AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00056};
DE AltName: Full=KDO-8-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00056};
DE Short=KDO 8-P synthase {ECO:0000255|HAMAP-Rule:MF_00056};
DE Short=KDOPS {ECO:0000255|HAMAP-Rule:MF_00056};
DE AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase {ECO:0000255|HAMAP-Rule:MF_00056};
GN Name=kdsA {ECO:0000255|HAMAP-Rule:MF_00056}; OrderedLocusNames=lpg1182;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
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:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_00056}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00056}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00056}.
CC -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000255|HAMAP-
CC Rule:MF_00056}.
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DR EMBL; AE017354; AAU27268.1; -; Genomic_DNA.
DR RefSeq; WP_010946916.1; NC_002942.5.
DR RefSeq; YP_095215.1; NC_002942.5.
DR PDB; 6MDY; X-ray; 2.55 A; A/B/C/D=1-274.
DR PDBsum; 6MDY; -.
DR AlphaFoldDB; Q5ZWA3; -.
DR SMR; Q5ZWA3; -.
DR STRING; 272624.lpg1182; -.
DR PaxDb; Q5ZWA3; -.
DR PRIDE; Q5ZWA3; -.
DR EnsemblBacteria; AAU27268; AAU27268; lpg1182.
DR GeneID; 66490360; -.
DR KEGG; lpn:lpg1182; -.
DR PATRIC; fig|272624.6.peg.1245; -.
DR eggNOG; COG2877; Bacteria.
DR HOGENOM; CLU_036666_0_0_6; -.
DR OMA; PHISQGV; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR Proteomes; UP000000609; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipopolysaccharide biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..274
FT /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT /id="PRO_0000187136"
FT STRAND 1..3
FT /evidence="ECO:0007829|PDB:6MDY"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:6MDY"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:6MDY"
FT HELIX 26..42
FT /evidence="ECO:0007829|PDB:6MDY"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:6MDY"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:6MDY"
FT HELIX 69..82
FT /evidence="ECO:0007829|PDB:6MDY"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6MDY"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:6MDY"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:6MDY"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:6MDY"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:6MDY"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:6MDY"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:6MDY"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:6MDY"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:6MDY"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:6MDY"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:6MDY"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:6MDY"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:6MDY"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:6MDY"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:6MDY"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:6MDY"
FT HELIX 253..270
FT /evidence="ECO:0007829|PDB:6MDY"
SQ SEQUENCE 274 AA; 29984 MW; 5A9668BB19CE3DFB CRC64;
MRLCGFEAGL DKPLFLIAGP CVIESEELAL ETAGYLKEMC SQLNIPFIYK SSFDKANRSS
ISSYRGPGFE KGLSILEKVK SQIGVPVLTD VHEDTPLFEV SSVVDVLQTP AFLCRQTNFI
QKVAAMNKPV NIKKGQFLAP WEMKHVIAKA KAQGNEQIMA CERGVSFGYN NLVSDMRSLV
IMRETGCPVV YDATHSVQLP GGNNGVSGGQ REFIPALARA AVAVGISGLF METHPDPDKA
LSDGPNSWPL DKMKQLLESL KAADEVYKKY STDF
