KDSC_SHIFL
ID KDSC_SHIFL Reviewed; 188 AA.
AC P67654; Q83JF3; Q8FD72;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=SF3238, S3456;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN44704.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18518.1; -; Genomic_DNA.
DR RefSeq; NP_708997.1; NC_004337.2.
DR RefSeq; WP_000030016.1; NZ_WPGW01000004.1.
DR AlphaFoldDB; P67654; -.
DR SMR; P67654; -.
DR STRING; 198214.SF3238; -.
DR EnsemblBacteria; AAN44704; AAN44704; SF3238.
DR EnsemblBacteria; AAP18518; AAP18518; S3456.
DR GeneID; 1027121; -.
DR GeneID; 58388197; -.
DR KEGG; sfl:SF3238; -.
DR KEGG; sfx:S3456; -.
DR PATRIC; fig|198214.7.peg.3839; -.
DR HOGENOM; CLU_106694_0_1_6; -.
DR OMA; VFMGVEN; -.
DR OrthoDB; 1232828at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00475.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000201701"
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; 20015 MW; 6A40ED8C20B1E3A7 CRC64;
MSKAGASLAT CYGPVSADVM AKAENIRLLI LDVDGVLSDG LIYMGNNGEE LKAFNVRDGY
GIRCALTSDI EVAIITGRKA KLVEDRCATL GITHLYQGQS NKLIAFSDLL EKLAIAPENV
AYVGDDLIDW PVMEKVGLSV AVADAHPLLI PRADYVTRIA GGRGAVREVC DLLLLAQGKL
DEAKGQSI
