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Database: UniProt
Entry: A0A0F4R3C8_9GAMM
LinkDB: A0A0F4R3C8_9GAMM
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ID   A0A0F4R3C8_9GAMM        Unreviewed;       185 AA.
AC   A0A0F4R3C8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=TW85_13590 {ECO:0000313|EMBL:KJZ13322.1};
OS   Marinomonas sp. S3726.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=579484 {ECO:0000313|EMBL:KJZ13322.1, ECO:0000313|Proteomes:UP000033747};
RN   [1] {ECO:0000313|EMBL:KJZ13322.1, ECO:0000313|Proteomes:UP000033747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S3726 {ECO:0000313|EMBL:KJZ13322.1,
RC   ECO:0000313|Proteomes:UP000033747};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(2015).
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:KJZ13322.1}.
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DR   EMBL; JXYC01000014; KJZ13322.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4R3C8; -.
DR   PATRIC; fig|579484.3.peg.2795; -.
DR   Proteomes; UP000033747; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033747}.
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   185 AA;  20504 MW;  7E7919747D4224A6 CRC64;
     MQFPENVLKK LQDLELVVFD VDGVLTDGGL LYGEQGETLK RFNVKDGVAL KLLPKWGVEV
     AIITAKDSAP LRKRMTDLSV KHFYPGCHNK KEAFLDLLKR LNITAGKAAY IGDDVIDLQV
     MPLVSLALCP NDAHVLVKRH CDMTLHCKAG EGVAREVCDL LLSSRMPLEN AYEIAQKPAF
     ESKSN
//
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