KDSC_ECOL6
ID KDSC_ECOL6 Reviewed; 188 AA.
AC P67653; Q83JF3; Q8FD72;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC;
DE EC=3.1.3.45 {ECO:0000269|PubMed:19726684};
DE AltName: Full=KDO 8-P phosphatase;
GN Name=kdsC; OrderedLocusNames=c3958;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2] {ECO:0007744|PDB:2R8E, ECO:0007744|PDB:2R8X, ECO:0007744|PDB:2R8Y, ECO:0007744|PDB:2R8Z, ECO:0007744|PDB:3HYC, ECO:0007744|PDB:3I6B}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
RP DIVALENT METALS, FUNCTION AS A KDO 8-P PHOSPHATASE, CATALYTIC ACTIVITY,
RP REACTION MECHANISM, COFACTOR, AND SUBUNIT.
RX PubMed=19726684; DOI=10.1074/jbc.m109.012278;
RA Biswas T., Yi L., Aggarwal P., Wu J., Rubin J.R., Stuckey J.A.,
RA Woodard R.W., Tsodikov O.V.;
RT "The tail of KdsC: conformational changes control the activity of a
RT haloacid dehalogenase superfamily phosphatase.";
RL J. Biol. Chem. 284:30594-30603(2009).
CC -!- FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-
CC phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic
CC phosphate. {ECO:0000269|PubMed:19726684}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-
CC deoxy-alpha-D-manno-oct-2-ulosonate + phosphate;
CC Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45;
CC Evidence={ECO:0000269|PubMed:19726684};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19726684};
CC -!- PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate
CC biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate:
CC step 3/3. {ECO:0000250|UniProtKB:A0A140N5J7}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000250|UniProtKB:A0A140N5J7}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19726684}.
CC -!- SIMILARITY: Belongs to the KdsC family. {ECO:0000305}.
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DR EMBL; AE014075; AAN82398.1; -; Genomic_DNA.
DR RefSeq; WP_000030016.1; NC_004431.1.
DR PDB; 2R8E; X-ray; 1.40 A; A/B/C/D/E/F/G/H=1-188.
DR PDB; 2R8X; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-188.
DR PDB; 2R8Y; X-ray; 1.85 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-188.
DR PDB; 2R8Z; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-188.
DR PDB; 3HYC; X-ray; 3.06 A; A/B/C/D/E/F/G/H=1-188.
DR PDB; 3I6B; X-ray; 2.49 A; A/B/C/D=1-180.
DR PDBsum; 2R8E; -.
DR PDBsum; 2R8X; -.
DR PDBsum; 2R8Y; -.
DR PDBsum; 2R8Z; -.
DR PDBsum; 3HYC; -.
DR PDBsum; 3I6B; -.
DR AlphaFoldDB; P67653; -.
DR SMR; P67653; -.
DR STRING; 199310.c3958; -.
DR EnsemblBacteria; AAN82398; AAN82398; c3958.
DR GeneID; 58388197; -.
DR KEGG; ecc:c3958; -.
DR eggNOG; COG1778; Bacteria.
DR HOGENOM; CLU_106694_0_1_6; -.
DR OMA; VFMGVEN; -.
DR BioCyc; ECOL199310:C3958-MON; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00475.
DR EvolutionaryTrace; P67653; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0019143; F:3-deoxy-manno-octulosonate-8-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR010023; KdsC_fam.
DR PIRSF; PIRSF006118; KDO8-P_Ptase; 1.
DR SFLD; SFLDG01138; C1.6.2:_Deoxy-d-mannose-octulo; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01670; KdsC-phosphatas; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Lipopolysaccharide biosynthesis; Magnesium;
KW Metal-binding.
FT CHAIN 1..188
FT /note="3-deoxy-D-manno-octulosonate 8-phosphate phosphatase
FT KdsC"
FT /id="PRO_0000201698"
FT BINDING 32
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19726684"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19726684"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19726684"
FT BINDING 55..59
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19726684"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19726684"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19726684"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19726684"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19726684"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19726684"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:2R8E"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:2R8E"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:2R8E"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:2R8E"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:2R8E"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:2R8E"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:2R8E"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:2R8E"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:2R8E"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2R8E"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:2R8E"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:2R8E"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:2R8E"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2R8E"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:2R8E"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:2R8E"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:2R8E"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2R8E"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:2R8E"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:2R8E"
FT HELIX 165..176
FT /evidence="ECO:0007829|PDB:2R8E"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:2R8Y"
SQ SEQUENCE 188 AA; 20015 MW; 6A40ED8C20B1E3A7 CRC64;
MSKAGASLAT CYGPVSADVM AKAENIRLLI LDVDGVLSDG LIYMGNNGEE LKAFNVRDGY
GIRCALTSDI EVAIITGRKA KLVEDRCATL GITHLYQGQS NKLIAFSDLL EKLAIAPENV
AYVGDDLIDW PVMEKVGLSV AVADAHPLLI PRADYVTRIA GGRGAVREVC DLLLLAQGKL
DEAKGQSI
