KDSC_ECOLI
ID KDSC_ECOLI Reviewed; 188 AA.
AC P0ABZ4; P45396; P45398; Q2M914;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC {ECO:0000250|UniProtKB:A0A140N5J7};
DE EC=3.1.3.45 {ECO:0000250|UniProtKB:A0A140N5J7};
DE AltName: Full=KDO 8-P phosphatase {ECO:0000250|UniProtKB:A0A140N5J7};
GN Name=kdsC {ECO:0000303|PubMed:16765569}; Synonyms=yrbI, yrbJ;
GN OrderedLocusNames=b3198, JW3165;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=16765569; DOI=10.1016/j.resmic.2005.11.014;
RA Sperandeo P., Pozzi C., Deho G., Polissi A.;
RT "Non-essential KDO biosynthesis and new essential cell envelope biogenesis
RT genes in the Escherichia coli yrbG-yhbG locus.";
RL Res. Microbiol. 157:547-558(2006).
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 -!- DISRUPTION PHENOTYPE: Not essential for growth.
CC {ECO:0000269|PubMed:16765569}.
CC -!- SIMILARITY: Belongs to the KdsC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA57999.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA58000.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA58000.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U18997; AAA57999.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U18997; AAA58000.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U00096; AAC76230.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77242.1; -; Genomic_DNA.
DR PIR; H65110; H65110.
DR RefSeq; NP_417665.1; NC_000913.3.
DR RefSeq; WP_000030005.1; NZ_SSZK01000007.1.
DR AlphaFoldDB; P0ABZ4; -.
DR SMR; P0ABZ4; -.
DR BioGRID; 4261882; 248.
DR DIP; DIP-48034N; -.
DR IntAct; P0ABZ4; 2.
DR STRING; 511145.b3198; -.
DR jPOST; P0ABZ4; -.
DR PaxDb; P0ABZ4; -.
DR PRIDE; P0ABZ4; -.
DR EnsemblBacteria; AAC76230; AAC76230; b3198.
DR EnsemblBacteria; BAE77242; BAE77242; BAE77242.
DR GeneID; 66672900; -.
DR GeneID; 947717; -.
DR KEGG; ecj:JW3165; -.
DR KEGG; eco:b3198; -.
DR PATRIC; fig|1411691.4.peg.3533; -.
DR EchoBASE; EB2656; -.
DR eggNOG; COG1778; Bacteria.
DR HOGENOM; CLU_106694_0_1_6; -.
DR InParanoid; P0ABZ4; -.
DR OMA; VFMGVEN; -.
DR PhylomeDB; P0ABZ4; -.
DR BioCyc; EcoCyc:G7663-MON; -.
DR SABIO-RK; P0ABZ4; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00475.
DR PRO; PR:P0ABZ4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:A0A140N5J7"
FT CHAIN 2..188
FT /note="3-deoxy-D-manno-octulosonate 8-phosphate phosphatase
FT KdsC"
FT /id="PRO_0000201696"
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
