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Database: UniProt
Entry: A0A1E5D2K5_9VIBR
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ID   A0A1E5D2K5_9VIBR        Unreviewed;       184 AA.
AC   A0A1E5D2K5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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   ORFNames=A130_14360 {ECO:0000313|EMBL:OEE77710.1};
OS   Vibrio genomosp. F6 str. FF-238.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1191298 {ECO:0000313|EMBL:OEE77710.1, ECO:0000313|Proteomes:UP000094165};
RN   [1] {ECO:0000313|EMBL:OEE77710.1, ECO:0000313|Proteomes:UP000094165}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FF-238 {ECO:0000313|EMBL:OEE77710.1,
RC   ECO:0000313|Proteomes:UP000094165};
RX   PubMed=22955834; DOI=10.1126/science.1219385;
RA   Cordero O.X., Wildschutte H., Kirkup B., Proehl S., Ngo L., Hussain F.,
RA   Le Roux F., Mincer T., Polz M.F.;
RT   "Ecological populations of bacteria act as socially cohesive units of
RT   antibiotic production and resistance.";
RL   Science 337:1228-1231(2012).
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:OEE77710.1}.
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DR   EMBL; AJYW02000073; OEE77710.1; -; Genomic_DNA.
DR   RefSeq; WP_017052624.1; NZ_AJYW02000073.1.
DR   AlphaFoldDB; A0A1E5D2K5; -.
DR   Proteomes; UP000094165; 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   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|PIRNR:PIRNR006118,
KW   ECO:0000256|PIRSR:PIRSR006118-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094165}.
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
FT   BINDING         15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
FT   BINDING         106
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
SQ   SEQUENCE   184 AA;  20137 MW;  8A77E121FA7EB2A3 CRC64;
     MVCFSQIEAV ILDVDGVMTD GSLNLDGYGE NFKSFNAKDG VAFELFRRNS IRVGVISGKS
     SESLNYRCKQ LGIDAVYSGC KLKVHALKNI CTTFDIEPKN IAFIGDDVID LPLFPLVGCA
     VPPSDAHALV KQKADLVLSS RGGDGAVREF VDMFLVEKNQ CTLDELYKPL IEDLIALSEI
     EVQQ
//
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