KDSA_VIBC3
ID KDSA_VIBC3 Reviewed; 283 AA.
AC A5F692; C3M3D2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 83.
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};
GN OrderedLocusNames=VC0395_A1752, VC395_2289;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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; CP000627; ABQ20781.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10281.1; -; Genomic_DNA.
DR RefSeq; WP_000400335.1; NZ_JAACZH010000001.1.
DR PDB; 3E9A; X-ray; 1.80 A; A=1-283.
DR PDBsum; 3E9A; -.
DR AlphaFoldDB; A5F692; -.
DR SMR; A5F692; -.
DR STRING; 345073.VC395_2289; -.
DR EnsemblBacteria; ABQ20781; ABQ20781; VC0395_A1752.
DR GeneID; 57740787; -.
DR KEGG; vco:VC0395_A1752; -.
DR KEGG; vcr:VC395_2289; -.
DR PATRIC; fig|345073.21.peg.2206; -.
DR eggNOG; COG2877; Bacteria.
DR HOGENOM; CLU_036666_0_0_6; -.
DR OMA; FRGIPTM; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR EvolutionaryTrace; A5F692; -.
DR Proteomes; UP000000249; Chromosome 2.
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; Transferase.
FT CHAIN 1..283
FT /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT /id="PRO_1000071154"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:3E9A"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:3E9A"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:3E9A"
FT HELIX 31..48
FT /evidence="ECO:0007829|PDB:3E9A"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:3E9A"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3E9A"
FT HELIX 74..88
FT /evidence="ECO:0007829|PDB:3E9A"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:3E9A"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:3E9A"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:3E9A"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:3E9A"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:3E9A"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:3E9A"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:3E9A"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:3E9A"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:3E9A"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:3E9A"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:3E9A"
FT HELIX 182..190
FT /evidence="ECO:0007829|PDB:3E9A"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:3E9A"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:3E9A"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:3E9A"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:3E9A"
FT STRAND 234..243
FT /evidence="ECO:0007829|PDB:3E9A"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:3E9A"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:3E9A"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:3E9A"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3E9A"
FT HELIX 260..276
FT /evidence="ECO:0007829|PDB:3E9A"
SQ SEQUENCE 283 AA; 30773 MW; D174E0105F98C09D CRC64;
MEHKIVHVGD IPVANDKPFT LFAGMNVLES RDLAMQICEH YVKVTDKLGI PYVFKASFDK
ANRSSVHSYR GPGLEEGMKI FQELKETFGV KIITDVHTEA QAQPVADVVD VIQLPAFLAR
QTDLVEAMAK TGAVINVKKP QFMSPGQVGN IVEKFAECGN DKVILCERGS CHGYDNLVVD
MLGFGVMKQA SNGSPIIFDV THSLQMRDPS GAASGGRREQ TVELAKAGLA TGIAGLFIEA
HPNPDKARCD GPSALPLDKL EPFLAQMKAL DDLIKSFAHI DIR
