ID E5VAC1_9BACE Unreviewed; 176 AA.
AC E5VAC1;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC {ECO:0000256|ARBA:ARBA00020092};
DE EC=3.1.3.45 {ECO:0000256|ARBA:ARBA00013066};
DE AltName: Full=KDO 8-P phosphatase {ECO:0000256|ARBA:ARBA00031051};
GN ORFNames=DXB40_05490 {ECO:0000313|EMBL:RGN84997.1}, DXD65_06145
GN {ECO:0000313|EMBL:RGJ35122.1}, HMPREF1007_01704
GN {ECO:0000313|EMBL:EFV26178.1};
OS Bacteroides sp. 4_1_36.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=457393 {ECO:0000313|EMBL:EFV26178.1, ECO:0000313|Proteomes:UP000004735};
RN [1] {ECO:0000313|EMBL:EFV26178.1, ECO:0000313|Proteomes:UP000004735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4_1_36 {ECO:0000313|EMBL:EFV26178.1,
RC ECO:0000313|Proteomes:UP000004735};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C.,
RA Allen-Vercoe E., Sibley C., Strauss J., Daigneault M., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides sp. strain 4_1_36.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000261007, ECO:0000313|Proteomes:UP000263804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OM03-9 {ECO:0000313|EMBL:RGN84997.1,
RC ECO:0000313|Proteomes:UP000261007}, and TM07-1
RC {ECO:0000313|EMBL:RGJ35122.1, ECO:0000313|Proteomes:UP000263804};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR006118-2};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the KdsC family.
CC {ECO:0000256|ARBA:ARBA00005893}.
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:EFV26178.1}.
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DR EMBL; ACTC01000064; EFV26178.1; -; Genomic_DNA.
DR EMBL; QSOX01000004; RGJ35122.1; -; Genomic_DNA.
DR EMBL; QSUY01000008; RGN84997.1; -; Genomic_DNA.
DR RefSeq; WP_005826358.1; NZ_QSOX01000004.1.
DR AlphaFoldDB; E5VAC1; -.
DR GeneID; 66280656; -.
DR HOGENOM; CLU_106694_1_0_10; -.
DR Proteomes; UP000004735; Unassembled WGS sequence.
DR Proteomes; UP000261007; Unassembled WGS sequence.
DR Proteomes; UP000263804; Unassembled WGS sequence.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
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; IPR041492; HAD_2.
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; PF13419; HAD_2; 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};
KW Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985};
KW Magnesium {ECO:0000256|PIRSR:PIRSR006118-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR006118-2}.
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
SQ SEQUENCE 176 AA; 19488 MW; 19C651796939A1AD CRC64;
MSTINYDLKK IKALVFDVDG VLSANVIPMS SEGEPLRTVN IKDGYSLHLA AKQGVLLGII
TGGRTEAVRK RFTSLGFEDG NIYMGSSVKI HDYHDFRDRH GLKDEEILYV GDDIPDLEVM
RECGLPCCPK DAVPEVKAVA RYISYAEGGY GCGRDIVEQV LKVQGLWMAD EKAFGW
//
