ID A0A3E0U7Y5_9GAMM Unreviewed; 188 AA.
AC A0A3E0U7Y5;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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:REL32657.1};
GN ORFNames=DXX94_07940 {ECO:0000313|EMBL:REL32657.1};
OS Thalassotalea euphylliae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassotalea.
OX NCBI_TaxID=1655234 {ECO:0000313|EMBL:REL32657.1, ECO:0000313|Proteomes:UP000256899};
RN [1] {ECO:0000313|Proteomes:UP000256899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3 {ECO:0000313|Proteomes:UP000256899};
RA Summers S., Rice S.A., Freckelton M.L., Nedved B.T., Hadfield M.G.;
RT "Thalassotalea euphylliae genome.";
RL Submitted (AUG-2018) 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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:REL32657.1}.
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DR EMBL; QUOT01000001; REL32657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E0U7Y5; -.
DR Proteomes; UP000256899; Unassembled WGS sequence.
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; SFLDS00003; Haloacid_Dehalogenase; 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|PIRNR:PIRNR006118,
KW ECO:0000256|PIRSR:PIRSR006118-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000256899}.
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:PIRSR006118-2"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
SQ SEQUENCE 188 AA; 20115 MW; 252DEAE8D5AADC24 CRC64;
MDTAQDLVST LYGPVAKQVI ATASNIKLLV CDVDGVFSDG RIYLGNQGEE LKAFHTKDGY
GIKALIASGV TVAIITGRNS RIVNDRMKAL NVEHIIQGKE DKLPEMKALM SELSITAEQV
AYIGDDMADL PCIEYAALGV AVNDAHPAVI NKADYRTFTL GGFGAVRELC DLIMHSQDTL
VDAKGASV
//
