KDSC_SALTI
ID KDSC_SALTI Reviewed; 188 AA.
AC Q8Z3G5;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC;
DE EC=3.1.3.45 {ECO:0000269|PubMed:25848029};
DE AltName: Full=KDO 8-P phosphatase;
GN Name=kdsC; OrderedLocusNames=STY3495, t3233;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=25848029; DOI=10.1073/pnas.1423570112;
RA Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L.,
RA Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D.,
RA Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., Dunaway-Mariano D.,
RA Allen K.N., Farelli J.D.;
RT "Panoramic view of a superfamily of phosphatases through substrate
RT profiling.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015).
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 in vitro. Also catalyzes the dephosphorylation of phospho-
CC tyrosine in vitro. {ECO:0000269|PubMed:25848029}.
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:25848029};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25848029};
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; AL513382; CAD07833.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70769.1; -; Genomic_DNA.
DR RefSeq; NP_457695.1; NC_003198.1.
DR RefSeq; WP_000030029.1; NZ_WSUR01000003.1.
DR AlphaFoldDB; Q8Z3G5; -.
DR SMR; Q8Z3G5; -.
DR STRING; 220341.16504381; -.
DR EnsemblBacteria; AAO70769; AAO70769; t3233.
DR KEGG; stt:t3233; -.
DR KEGG; sty:STY3495; -.
DR PATRIC; fig|220341.7.peg.3559; -.
DR eggNOG; COG1778; Bacteria.
DR HOGENOM; CLU_106694_0_1_6; -.
DR OMA; VFMGVEN; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00475.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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 1: Evidence at protein level;
KW Hydrolase; Lipopolysaccharide biosynthesis; Magnesium; Metal-binding.
FT CHAIN 1..188
FT /note="3-deoxy-D-manno-octulosonate 8-phosphate phosphatase
FT KdsC"
FT /id="PRO_0000201699"
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; 20075 MW; ADEFB0323DBFEF43 CRC64;
MSKAGASLAT CYGPVSTHVM TKAENIRLLI LDVDGVLSDG LIYMGNNGEE LKAFNVRDGY
GIRCALTSNI EVAIITGRKA KLVEDRCATL GIVHLYQGQS NKLIAFSDLL EKLAIAPENV
AYVGDDLIDW PVMEKVGLSV AVADAHPLLI PRADYVTHIA GGRGAVREVC DLLLLAQGKL
DEAKGQSI
