KDSC_YERPE
ID KDSC_YERPE Reviewed; 187 AA.
AC Q8ZB47; Q0WB73;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=YPO3578, y0150, YP_3833;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), AND SUBUNIT.
RA Papazisi L., Anderson W.F.;
RT "1.95 angstrom resolution crystal structure of 3-deoxy-d- manno-
RT octulosonate 8-phosphate phosphatase from Yersinia pestis.";
RL Submitted (AUG-2009) to the PDB data bank.
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; AL590842; CAL22166.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM83744.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS63980.1; -; Genomic_DNA.
DR PIR; AC0435; AC0435.
DR RefSeq; WP_002228203.1; NZ_WUCM01000032.1.
DR RefSeq; YP_002348465.1; NC_003143.1.
DR PDB; 3IJ5; X-ray; 1.95 A; A/B/C/D=1-187.
DR PDBsum; 3IJ5; -.
DR AlphaFoldDB; Q8ZB47; -.
DR SMR; Q8ZB47; -.
DR STRING; 214092.YPO3578; -.
DR PaxDb; Q8ZB47; -.
DR DNASU; 1145097; -.
DR EnsemblBacteria; AAM83744; AAM83744; y0150.
DR EnsemblBacteria; AAS63980; AAS63980; YP_3833.
DR GeneID; 66844059; -.
DR KEGG; ype:YPO3578; -.
DR KEGG; ypk:y0150; -.
DR KEGG; ypm:YP_3833; -.
DR PATRIC; fig|214092.21.peg.4072; -.
DR eggNOG; COG1778; Bacteria.
DR HOGENOM; CLU_106694_0_1_6; -.
DR OMA; VFMGVEN; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00475.
DR EvolutionaryTrace; Q8ZB47; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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 3D-structure; Hydrolase; Lipopolysaccharide biosynthesis; Magnesium;
KW Metal-binding; Reference proteome.
FT CHAIN 1..187
FT /note="3-deoxy-D-manno-octulosonate 8-phosphate phosphatase
FT KdsC"
FT /id="PRO_0000201702"
FT BINDING 31
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 33
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 54..58
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:3IJ5"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:3IJ5"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:3IJ5"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:3IJ5"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:3IJ5"
FT HELIX 55..66
FT /evidence="ECO:0007829|PDB:3IJ5"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:3IJ5"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:3IJ5"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:3IJ5"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:3IJ5"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:3IJ5"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:3IJ5"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3IJ5"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:3IJ5"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:3IJ5"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:3IJ5"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:3IJ5"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:3IJ5"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:3IJ5"
FT HELIX 164..175
FT /evidence="ECO:0007829|PDB:3IJ5"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:3IJ5"
SQ SEQUENCE 187 AA; 20299 MW; 299EA75C7DEA7878 CRC64;
MSNTAYIDTC YGPVADDVIQ RAANIRLLIC DVDGVMSDGL IYMGNQGEEL KAFNVRDGYG
IRCLITSDID VAIITGRRAK LLEDRANTLG ITHLYQGQSD KLVAYHELLA TLQCQPEQVA
YIGDDLIDWP VMAQVGLSVA VADAHPLLLP KAHYVTRIKG GRGAVREVCD LILLAQDKLE
GATGLSI
