ID H1G0N7_9GAMM Unreviewed; 175 AA.
AC H1G0N7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=ECTPHS_01699 {ECO:0000313|EMBL:EHQ51374.1};
OS Ectothiorhodospira sp. PHS-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=519989 {ECO:0000313|EMBL:EHQ51374.1, ECO:0000313|Proteomes:UP000005314};
RN [1] {ECO:0000313|EMBL:EHQ51374.1, ECO:0000313|Proteomes:UP000005314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHS-1 {ECO:0000313|EMBL:EHQ51374.1,
RC ECO:0000313|Proteomes:UP000005314};
RA Saltikov C.W., Zargar K., Conrad A., Bernick D., Lowe T.M., Stolc V.,
RA Hoeft S., Oremland R.S., Stolz J.;
RT "ArxA, a new clade of arsenite oxidase within the DMSO family of molybdenum
RT oxidoreductases.";
RL Submitted (JAN-2012) 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:EHQ51374.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGBG01000003; EHQ51374.1; -; Genomic_DNA.
DR RefSeq; WP_008930941.1; NZ_AGBG01000003.1.
DR AlphaFoldDB; H1G0N7; -.
DR STRING; 519989.ECTPHS_01699; -.
DR PATRIC; fig|519989.5.peg.340; -.
DR eggNOG; COG1778; Bacteria.
DR OrthoDB; 9805604at2; -.
DR Proteomes; UP000005314; 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; SFLDF00036; deoxy-d-mannose-octulosonate_8; 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 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-1"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-1"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-1"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-1"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-1"
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
SQ SEQUENCE 175 AA; 19027 MW; 0F40C1713A5996F5 CRC64;
MNETLTERAR RVRFVIFDVD GVLTDGSLFL DDDGRQYKAF NSKDGQGMRM LADSGVQVGI
LTGRRSGVVE HRMRDLGIRL VVQGRRDKLE ALGGLLADAG VGADETAYVG DDVVDLPVMR
RVALAVAVAD AHALVREHAH YVTRQPGGRG AAREVCEFIM EAQGTLQAAM AAYLR
//
