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Database: UniProt
Entry: A0A0X3Y9M1_9GAMM
LinkDB: A0A0X3Y9M1_9GAMM
Original site: A0A0X3Y9M1_9GAMM 
ID   A0A0X3Y9M1_9GAMM        Unreviewed;       184 AA.
AC   A0A0X3Y9M1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=AR688_06480 {ECO:0000313|EMBL:KUM53546.1};
OS   Rheinheimera sp. EpRS3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Rheinheimera.
OX   NCBI_TaxID=1712383 {ECO:0000313|EMBL:KUM53546.1, ECO:0000313|Proteomes:UP000054239};
RN   [1] {ECO:0000313|Proteomes:UP000054239}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS3 {ECO:0000313|Proteomes:UP000054239};
RA   Presta L., Bosi E., Fondi M., Maida I., Maggini V., Bogani P.,
RA   Firenzuoli F., Chiellini C., De Pascale D., Palma F., Di Pilato V.,
RA   Rossolini G., Mengoni A., Fani R.;
RL   Submitted (NOV-2015) 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:KUM53546.1}.
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DR   EMBL; LNQS01000008; KUM53546.1; -; Genomic_DNA.
DR   RefSeq; WP_068233934.1; NZ_LNQS01000008.1.
DR   AlphaFoldDB; A0A0X3Y9M1; -.
DR   OrthoDB; 9805604at2; -.
DR   Proteomes; UP000054239; 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; 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}.
FT   BINDING         28
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
FT   BINDING         30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
FT   BINDING         121
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
SQ   SEQUENCE   184 AA;  20284 MW;  71C0CD1674A80FB5 CRC64;
     MSLFNTLYQP VSDSIIHKAR AIKLLICDVD GVFSDGRIYL GNQGEELKAF HTRDGYGVKA
     LRQAKVEVAV ITGRNSAIVQ QRMTALTVPF IYQGQENKLA AFADLQQQLQ LTPEQIAYIG
     DDLPDWAVMQ HCGLSVAVKD AHPYLRQHAN YITAMAGGFG AVREICDLIL ISQQHFGLFD
     GSSS
//
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