ID G2FF74_9GAMM Unreviewed; 173 AA.
AC G2FF74;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
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:EGW54621.1};
GN ORFNames=TevJSym_ak00850 {ECO:0000313|EMBL:EGW54621.1};
OS endosymbiont of Tevnia jerichonana (vent Tica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW54621.1, ECO:0000313|Proteomes:UP000005167};
RN [1] {ECO:0000313|EMBL:EGW54621.1, ECO:0000313|Proteomes:UP000005167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA Sievert S.M., Schweder T.;
RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT jerichonana share an identical physiology as revealed by proteogenomic
RT analyses.";
RL ISME J. 0:0-0(2011).
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:EGW54621.1}.
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DR EMBL; AFZB01000011; EGW54621.1; -; Genomic_DNA.
DR RefSeq; WP_005959865.1; NZ_AFZB01000011.1.
DR AlphaFoldDB; G2FF74; -.
DR PATRIC; fig|1049564.3.peg.1556; -.
DR eggNOG; COG1778; Bacteria.
DR Proteomes; UP000005167; 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; 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; SFLDF00036; deoxy-d-mannose-octulosonate_8; 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:UP000005167}.
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
FT BINDING 110
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
SQ SEQUENCE 173 AA; 19216 MW; 8F9FD6FFFA357303 CRC64;
MQDIQEKARR IRLVIFDVDG VLTDGSLFLG DDGQEYKAFN SRDGHGIKML QQSGIEIGII
TGRSSEVVRL RMQSLGIKHV YQGQLDKRPA YQELRDKLGL SDAEIAYVGD DVVDLPIMRL
VGLAIAVNDA HPFVTQHAHW LTPHAGGRGA ARDVCELLMD AQGHLQRVLQ SYL
//