(data stored in SCRATCH zone)

SWISSPROT: C5B732_EDWI9

ID   C5B732_EDWI9            Unreviewed;       188 AA.
AC   C5B732;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 54.
DE   RecName: Full=3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC {ECO:0000256|PIRNR:PIRNR006118};
DE            EC=3.1.3.45 {ECO:0000256|PIRNR:PIRNR006118};
DE   AltName: Full=KDO 8-P phosphatase {ECO:0000256|PIRNR:PIRNR006118};
GN   OrderedLocusNames=NT01EI_0577 {ECO:0000313|EMBL:ACR67806.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67806.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of lipopolysaccharides
CC       (LPSs). Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate
CC       8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and
CC       inorganic phosphate. {ECO:0000256|PIRNR:PIRNR006118}.
CC   -!- CATALYTIC ACTIVITY: 3-deoxy-D-manno-octulosonate 8-phosphate +
CC       H(2)O = 3-deoxy-D-manno-octulosonate + phosphate.
CC       {ECO:0000256|PIRNR:PIRNR006118}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006118,
CC         ECO:0000256|PIRSR:PIRSR006118-2};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000256|PIRNR:PIRNR006118}.
CC   -!- PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate
CC       biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-
CC       phosphate: step 3/3. {ECO:0000256|PIRNR:PIRNR006118}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR006118}.
CC   -!- SIMILARITY: Belongs to the KdsC family.
CC       {ECO:0000256|PIRNR:PIRNR006118}.
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DR   EMBL; CP001600; ACR67806.1; -; Genomic_DNA.
DR   RefSeq; WP_015870005.1; NC_012779.2.
DR   ProteinModelPortal; C5B732; -.
DR   STRING; 634503.NT01EI_0577; -.
DR   EnsemblBacteria; ACR67806; ACR67806; NT01EI_0577.
DR   GeneID; 7960345; -.
DR   KEGG; eic:NT01EI_0577; -.
DR   PATRIC; fig|634503.3.peg.522; -.
DR   eggNOG; ENOG4108Z4R; Bacteria.
DR   eggNOG; COG1778; LUCA.
DR   HOGENOM; HOG000264740; -.
DR   KO; K03270; -.
DR   OMA; CVGDDYN; -.
DR   OrthoDB; POG091H01V2; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00475.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0019143; F:3-deoxy-manno-octulosonate-8-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR010023; KDO_8-P_phosphatase.
DR   Pfam; PF08282; Hydrolase_3; 1.
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; TIGR01662; HAD-SF-IIIA; 1.
DR   TIGRFAMs; TIGR01670; KdsC-phosphatas; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B732.
DR   SWISS-2DPAGE; C5B732.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006118,
KW   ECO:0000256|SAAS:SAAS00078030, ECO:0000313|EMBL:ACR67806.1};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|PIRNR:PIRNR006118};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR006118,
KW   ECO:0000256|PIRSR:PIRSR006118-2};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR006118,
KW   ECO:0000256|PIRSR:PIRSR006118-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN       95    158       HAD-like_dom. {ECO:0000259|Pfam:PF08282}.
FT   METAL        32     32       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR006118-2}.
FT   METAL        34     34       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR006118-2}.
FT   METAL       125    125       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR006118-2}.
FT   BINDING      34     34       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006118-1}.
FT   BINDING      63     63       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006118-1}.
FT   BINDING      78     78       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006118-1}.
FT   BINDING      86     86       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006118-1}.
FT   BINDING     102    102       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006118-1}.
SQ   SEQUENCE   188 AA;  20119 MW;  3D6E75C0A6F4179D CRC64;
     MQQNTSPIAT CYGPVPADVM ARATQIRLLI CDVDGVLSDG LIYMGNQGEE LKAFNVRDGY
     GIRCLVTQGI EVAIITGRSS QLVADRAATL GIRHLYQGQS DKLIAFEHIL ADLQLAPHQA
     AYIGDDLIDW PVMARVGLSV AVADAHPLLL PNAHYTTRIA GGRGAVRELC DIILQAQGCL
     SQAKGLSI
//

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