KDSA_PSEAE
ID KDSA_PSEAE Reviewed; 281 AA.
AC Q9ZFK4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=PA3636;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Walsh A.G., Burrows L.L., Lam J.S.;
RT "kdsA gene of Pseudomonas aeruginosa PAO1.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(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; AF098791; AAD13217.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07024.1; -; Genomic_DNA.
DR PIR; A83192; A83192.
DR RefSeq; NP_252326.1; NC_002516.2.
DR RefSeq; WP_003092365.1; NZ_QZGE01000001.1.
DR PDB; 4LU0; X-ray; 2.80 A; A/B/C/D=2-281.
DR PDBsum; 4LU0; -.
DR AlphaFoldDB; Q9ZFK4; -.
DR SMR; Q9ZFK4; -.
DR STRING; 287.DR97_4303; -.
DR PaxDb; Q9ZFK4; -.
DR PRIDE; Q9ZFK4; -.
DR DNASU; 880428; -.
DR EnsemblBacteria; AAG07024; AAG07024; PA3636.
DR GeneID; 880428; -.
DR KEGG; pae:PA3636; -.
DR PATRIC; fig|208964.12.peg.3805; -.
DR PseudoCAP; PA3636; -.
DR HOGENOM; CLU_036666_0_0_6; -.
DR InParanoid; Q9ZFK4; -.
DR OMA; FRGIPTM; -.
DR PhylomeDB; Q9ZFK4; -.
DR BioCyc; PAER208964:G1FZ6-3706-MON; -.
DR BRENDA; 2.5.1.55; 5087.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IDA:PseudoCAP.
DR GO; GO:0008676; F:3-deoxy-8-phosphooctulonate synthase activity; IBA:GO_Central.
DR GO; GO:0015976; P:carbon utilization; IDA:PseudoCAP.
DR GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IDA:PseudoCAP.
DR GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IDA:PseudoCAP.
DR GO; GO:0046364; P:monosaccharide biosynthetic process; IBA:GO_Central.
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..281
FT /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT /id="PRO_0000187150"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:4LU0"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:4LU0"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:4LU0"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:4LU0"
FT HELIX 31..48
FT /evidence="ECO:0007829|PDB:4LU0"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:4LU0"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:4LU0"
FT HELIX 73..88
FT /evidence="ECO:0007829|PDB:4LU0"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:4LU0"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4LU0"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:4LU0"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:4LU0"
FT TURN 116..120
FT /evidence="ECO:0007829|PDB:4LU0"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:4LU0"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:4LU0"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:4LU0"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:4LU0"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:4LU0"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:4LU0"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:4LU0"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:4LU0"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:4LU0"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:4LU0"
FT HELIX 258..273
FT /evidence="ECO:0007829|PDB:4LU0"
SQ SEQUENCE 281 AA; 31143 MW; 7AAED3D4C0EEFA99 CRC64;
MAQKIVRVGD IQIGNDLPFV LFGGMNVLES RDLAMQVCEE YVRVTEKLGI PYVFKASFDK
ANRSSIHSFR GPGLEEGMKI FEEIKKTFKV PVITDVHEPF QAQPVAEVCD IIQLPAFLSR
QTDLVVAMAR TNAVINIKKA QFLAPQEMKH ILTKCEEAGN DRLILCERGS SFGYNNLVVD
MLGFGIMKQF EYPVFFDVTH ALQMPGGRAD SAGGRRAQVT DLAKAGLSQK LAGLFLEAHP
DPEHAKCDGP CALRLNKLEA FLSQLKQLDE LIKSFPAIET A
