ID A0A0M2KK04_9GAMM Unreviewed; 188 AA.
AC A0A0M2KK04;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC {ECO:0000256|ARBA:ARBA00020092, ECO:0000256|PIRNR:PIRNR006118};
DE EC=3.1.3.45 {ECO:0000256|ARBA:ARBA00013066, ECO:0000256|PIRNR:PIRNR006118};
DE AltName: Full=KDO 8-P phosphatase {ECO:0000256|ARBA:ARBA00031051, ECO:0000256|PIRNR:PIRNR006118};
GN Name=kdsC {ECO:0000313|EMBL:AXF78278.1};
GN ORFNames=AV903_23335 {ECO:0000313|EMBL:AXF78278.1}, SY86_21105
GN {ECO:0000313|EMBL:KKF37341.1};
OS Erwinia tracheiphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=65700 {ECO:0000313|EMBL:KKF37341.1, ECO:0000313|Proteomes:UP000033924};
RN [1] {ECO:0000313|EMBL:KKF37341.1, ECO:0000313|Proteomes:UP000033924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BuffGH {ECO:0000313|EMBL:KKF37341.1,
RC ECO:0000313|Proteomes:UP000033924};
RA Shapiro L.R.;
RT "Erwinia tracheiphila.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AXF78278.1, ECO:0000313|Proteomes:UP000264980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDcuke {ECO:0000313|EMBL:AXF78278.1,
RC ECO:0000313|Proteomes:UP000264980};
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|PIRNR:PIRNR006118}.
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:0000256|ARBA:ARBA00000898,
CC ECO:0000256|PIRNR:PIRNR006118};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR006118, ECO:0000256|PIRSR:PIRSR006118-2};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004756,
CC ECO:0000256|PIRNR:PIRNR006118}.
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:0000256|ARBA:ARBA00004807,
CC ECO:0000256|PIRNR:PIRNR006118}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|PIRNR:PIRNR006118}.
CC -!- SIMILARITY: Belongs to the KdsC family. {ECO:0000256|ARBA:ARBA00005893,
CC ECO:0000256|PIRNR:PIRNR006118}.
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DR EMBL; CP013970; AXF78278.1; -; Genomic_DNA.
DR EMBL; JXNU01000003; KKF37341.1; -; Genomic_DNA.
DR RefSeq; WP_016190567.1; NZ_JXNU01000003.1.
DR AlphaFoldDB; A0A0M2KK04; -.
DR STRING; 65700.SY86_21105; -.
DR PATRIC; fig|65700.7.peg.5265; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00475.
DR Proteomes; UP000033924; Unassembled WGS sequence.
DR Proteomes; UP000264980; 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 CDD; cd01630; HAD_KDO-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR010023; KdsC_fam.
DR NCBIfam; TIGR01670; KdsC-phosphatas; 1.
DR PANTHER; PTHR21485:SF5; 3-DEOXY-D-MANNO-OCTULOSONATE 8-PHOSPHATE PHOSPHATASE KDSC; 1.
DR PANTHER; PTHR21485; HAD SUPERFAMILY MEMBERS CMAS AND KDSC; 1.
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 SFLD; SFLDG01136; C1.6:_Phosphoserine_Phosphatas; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR006118};
KW Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985,
KW ECO:0000256|PIRNR:PIRNR006118};
KW Magnesium {ECO:0000256|PIRNR:PIRNR006118, ECO:0000256|PIRSR:PIRSR006118-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR006118};
KW Reference proteome {ECO:0000313|Proteomes:UP000033924}.
FT BINDING 32
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-1"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-1"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-1"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-1"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-1"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
SQ SEQUENCE 188 AA; 20727 MW; 3F6CF140F23C4AE3 CRC64;
MSTVVNWTET CYGKVSLEVM NRAKKIKLLI CDVDGVMSDG VIYQGNNGEE LKAFNVRDGY
GIRCLLTSDV EVAIITGRKA KLLEDRCTTL GISHLYQDQP DKILAFRELL DKLSLQPEQV
AYIGDDLIDW PVMAQVGLSV TVADAHPVLI PRANYVTRIA GGRGAVREIC DLLLIAQDKF
DEAKGQSV
//
