KDSC_ECO57
ID KDSC_ECO57 Reviewed; 188 AA.
AC P0ABZ5; P45396; P45398;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC;
DE EC=3.1.3.45 {ECO:0000250|UniProtKB:A0A140N5J7};
DE AltName: Full=KDO 8-P phosphatase;
GN Name=kdsC; OrderedLocusNames=Z4561, ECs4077;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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:0000250|UniProtKB:A0A140N5J7}.
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:0000250|UniProtKB:A0A140N5J7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A140N5J7};
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:0000250|UniProtKB:A0A140N5J7}.
CC -!- SIMILARITY: Belongs to the KdsC family. {ECO:0000305}.
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DR EMBL; AE005174; AAG58332.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37500.1; -; Genomic_DNA.
DR PIR; E91138; E91138.
DR PIR; H85983; H85983.
DR RefSeq; NP_312104.1; NC_002695.1.
DR RefSeq; WP_000030005.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0ABZ5; -.
DR SMR; P0ABZ5; -.
DR STRING; 155864.EDL933_4426; -.
DR EnsemblBacteria; AAG58332; AAG58332; Z4561.
DR EnsemblBacteria; BAB37500; BAB37500; ECs_4077.
DR GeneID; 66672900; -.
DR GeneID; 916077; -.
DR KEGG; ece:Z4561; -.
DR KEGG; ecs:ECs_4077; -.
DR PATRIC; fig|386585.9.peg.4256; -.
DR eggNOG; COG1778; Bacteria.
DR HOGENOM; CLU_106694_0_1_6; -.
DR OMA; VFMGVEN; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00475.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0019143; F:3-deoxy-manno-octulosonate-8-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Hydrolase; Lipopolysaccharide biosynthesis; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..188
FT /note="3-deoxy-D-manno-octulosonate 8-phosphate phosphatase
FT KdsC"
FT /id="PRO_0000201697"
FT BINDING 32
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 55..59
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P67653"
SQ SEQUENCE 188 AA; 19997 MW; 75AF512CF4E5E6E2 CRC64;
MSKAGASLAT CYGPVSADVI AKAENIRLLI LDVDGVLSDG LIYMGNNGEE LKAFNVRDGY
GIRCALTSDI EVAIITGRKA KLVEDRCATL GITHLYQGQS NKLIAFSDLL EKLAIAPENV
AYVGDDLIDW PVMEKVGLSV AVADAHPLLI PRADYVTRIA GGRGAVREVC DLLLLAQGKL
DEAKGQSI
