ID A0A0P1LR17_9BACT Unreviewed; 168 AA.
AC A0A0P1LR17; A0A0P1LDJ2; A0A0P1LLG1; A0A0P1LMF7; A0A0P1LPA8; A0A0P1LZ28;
AC A0A0P1MBF6; A0A0P1MMD0; A0A0P1MNP4; A0A0P1P2I3; A0A0S4MU97;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC {ECO:0000256|ARBA:ARBA00020092};
DE EC=3.1.3.45 {ECO:0000256|ARBA:ARBA00013066};
DE AltName: Full=KDO 8-P phosphatase {ECO:0000256|ARBA:ARBA00031051};
GN ORFNames=JGI4_00477 {ECO:0000313|EMBL:CUU02309.1};
OS Candidatus Kryptonium thompsoni.
OC Bacteria; Candidatus Kryptonia; Kryptonium.
OX NCBI_TaxID=1633631 {ECO:0000313|EMBL:CUU02309.1, ECO:0000313|Proteomes:UP000182011};
RN [1] {ECO:0000313|EMBL:CUU02309.1, ECO:0000313|Proteomes:UP000182011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JGI-4 {ECO:0000313|EMBL:CUU02309.1};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR006118-2};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the KdsC family.
CC {ECO:0000256|ARBA:ARBA00005893}.
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DR EMBL; FAOP01000003; CUU02309.1; -; Genomic_DNA.
DR RefSeq; WP_047133831.1; NZ_CZVX01000105.1.
DR AlphaFoldDB; A0A0P1LR17; -.
DR STRING; 1633631.GCA_001442925_00477; -.
DR OrthoDB; 9805604at2; -.
DR Proteomes; UP000182011; Unassembled WGS sequence.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
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; IPR006549; HAD-SF_hydro_IIIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR010023; KdsC_fam.
DR NCBIfam; TIGR01662; HAD-SF-IIIA; 1.
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};
KW Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985};
KW Magnesium {ECO:0000256|PIRSR:PIRSR006118-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR006118-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000182011}.
FT BINDING 20
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
SQ SEQUENCE 168 AA; 18254 MW; AC146927A4F0627F CRC64;
MKVRKGATEK AQKVKMILLD VDGVLTDGSI IYSSNCGEIK VFNAQDGFGI VRAIELGLKV
GIITGRESDI IKKRANELGI TDLIQNAIDK VKPFETLASK YNLKPEQFCY VGDDILDIPL
LKIVGFSAAP ANARSEVKRV VDYVASASGG NGAVREIIDF ILRAQKKI
//
