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Database: UniProt
Entry: A0A1Q9HC05_9VIBR
LinkDB: A0A1Q9HC05_9VIBR
Original site: A0A1Q9HC05_9VIBR 
ID   A0A1Q9HC05_9VIBR        Unreviewed;       185 AA.
AC   A0A1Q9HC05;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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:KAB1455457.1};
GN   ORFNames=BIY22_10060 {ECO:0000313|EMBL:OLQ86922.1}, F7O85_21820
GN   {ECO:0000313|EMBL:KAB1455457.1};
OS   Vibrio panuliri.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1381081 {ECO:0000313|EMBL:OLQ86922.1, ECO:0000313|Proteomes:UP000186313};
RN   [1] {ECO:0000313|EMBL:OLQ86922.1, ECO:0000313|Proteomes:UP000186313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAIM 703 {ECO:0000313|EMBL:OLQ86922.1,
RC   ECO:0000313|Proteomes:UP000186313};
RA   Gonzalez-Castillo A., Gomez-Gil B., Enciso-Ibarra K.;
RT   "Genomic Taxonomy of the Vibrionaceae.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAB1455457.1, ECO:0000313|Proteomes:UP000446972}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LBS 2 {ECO:0000313|EMBL:KAB1455457.1,
RC   ECO:0000313|Proteomes:UP000446972};
RA   Das S.S.;
RT   "Whole genome sequence of Vibrio panuliri LBS 2.";
RL   Submitted (SEP-2019) 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:OLQ86922.1}.
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DR   EMBL; WAHU01000009; KAB1455457.1; -; Genomic_DNA.
DR   EMBL; MJMJ01000034; OLQ86922.1; -; Genomic_DNA.
DR   RefSeq; WP_075709737.1; NZ_WAHU01000009.1.
DR   AlphaFoldDB; A0A1Q9HC05; -.
DR   STRING; 1381081.BIY22_10060; -.
DR   OrthoDB; 9805604at2; -.
DR   Proteomes; UP000186313; Unassembled WGS sequence.
DR   Proteomes; UP000446972; 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; 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}.
FT   BINDING         29
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
FT   BINDING         31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
FT   BINDING         122
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
SQ   SEQUENCE   185 AA;  20376 MW;  7BC0BEFA4F7656AB CRC64;
     MTTKVATLYG QVDTEILEIA KQIKLLICDV DGVFSDGLIY MGNNGEELKT FHTRDGYGVK
     SLMNAGIEIA IITGRRSQIV ENRMTALGIS LIYQGQDDKV KAYQDICQKL NIAPEQTGYI
     GDDLIDWPVM EKVALKVCVA DGHPLLAQRA NYVTNIRGGH GAVREVCDLI LQARNELDVH
     KGLSI
//
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