KDSC_ECOBD
ID KDSC_ECOBD Reviewed; 188 AA.
AC A0A140N5J7;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC {ECO:0000303|PubMed:12639950};
DE EC=3.1.3.45 {ECO:0000269|PubMed:12639950};
DE AltName: Full=KDO 8-P phosphatase {ECO:0000303|PubMed:12639950};
GN Name=kdsC {ECO:0000250|UniProtKB:P0ABZ4};
GN OrderedLocusNames=ECBD_0544 {ECO:0000312|EMBL:ACT27614.1};
OS Escherichia coli (strain B / BL21-DE3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=469008;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B / BL21-DE3;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.;
RT "Complete sequence of Escherichia coli BL21(DE3).";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-10, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, PATHWAY, MASS
RP SPECTROMETRY, AND SUBUNIT.
RC STRAIN=B / BL21-DE3;
RX PubMed=12639950; DOI=10.1074/jbc.m301983200;
RA Wu J., Woodard R.W.;
RT "Escherichia coli YrbI is 3-deoxy-D-manno-octulosonate 8-phosphate
RT phosphatase.";
RL J. Biol. Chem. 278:18117-18123(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:0000269|PubMed:12639950}.
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:12639950};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12639950};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:12639950};
CC Note=Mg(2+). The phosphatase activity is also stimulated by cobalt
CC ions, whereas baryum, zinc, and manganese ions are less effective
CC stimulators. {ECO:0000269|PubMed:12639950};
CC -!- ACTIVITY REGULATION: Inhibited by calcium, cadmium, mercury, and copper
CC ions. {ECO:0000269|PubMed:12639950}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=75 uM for KDO 8-P {ECO:0000269|PubMed:12639950};
CC Vmax=500 umol/min/mg enzyme {ECO:0000269|PubMed:12639950};
CC Note=kcat is 175 sec(-1). {ECO:0000269|PubMed:12639950};
CC pH dependence:
CC Optimum pH is 5.5. High catalytic activity is observed between pH 5.5
CC and 7.0. {ECO:0000269|PubMed:12639950};
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:0000305|PubMed:12639950}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000305|PubMed:12639950}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12639950}.
CC -!- MASS SPECTROMETRY: Mass=19881; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12639950};
CC -!- SIMILARITY: Belongs to the KdsC family. {ECO:0000305}.
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DR EMBL; CP001665; ACT27614.1; -; Genomic_DNA.
DR RefSeq; WP_000030016.1; NZ_CP053602.1.
DR AlphaFoldDB; A0A140N5J7; -.
DR SMR; A0A140N5J7; -.
DR STRING; 469008.B21_03014; -.
DR GeneID; 58388197; -.
DR KEGG; ebd:ECBD_0544; -.
DR PATRIC; fig|469008.15.peg.3103; -.
DR eggNOG; COG1778; Bacteria.
DR HOGENOM; CLU_106694_0_1_6; -.
DR OMA; VFMGVEN; -.
DR BioCyc; MetaCyc:GCQ7-3299-MON; -.
DR SABIO-RK; A0A140N5J7; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00475.
DR Proteomes; UP000002032; 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 Direct protein sequencing; Hydrolase; Lipopolysaccharide biosynthesis;
KW Magnesium; Metal-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12639950"
FT CHAIN 2..188
FT /note="3-deoxy-D-manno-octulosonate 8-phosphate phosphatase
FT KdsC"
FT /id="PRO_0000444889"
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
