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Database: UniProt
Entry: Q8RGS1_FUSNN
LinkDB: Q8RGS1_FUSNN
Original site: Q8RGS1_FUSNN 
ID   Q8RGS1_FUSNN            Unreviewed;       168 AA.
AC   Q8RGS1;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 112.
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   OrderedLocusNames=FN0213 {ECO:0000313|EMBL:AAL94419.1};
OS   Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS   BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC   Fusobacterium.
OX   NCBI_TaxID=190304 {ECO:0000313|EMBL:AAL94419.1, ECO:0000313|Proteomes:UP000002521};
RN   [1] {ECO:0000313|EMBL:AAL94419.1, ECO:0000313|Proteomes:UP000002521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 /
RC   KCTC 2640 / LMG 13131 / VPI 4355 {ECO:0000313|Proteomes:UP000002521};
RX   PubMed=11889109; DOI=10.1128/JB.184.7.2005-2018.2002;
RA   Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA   Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA   Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA   Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N., Overbeek R.;
RT   "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT   strain ATCC 25586.";
RL   J. Bacteriol. 184:2005-2018(2002).
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}.
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DR   EMBL; AE009951; AAL94419.1; -; Genomic_DNA.
DR   RefSeq; NP_603120.1; NC_003454.1.
DR   RefSeq; WP_011016229.1; NZ_CP028101.1.
DR   AlphaFoldDB; Q8RGS1; -.
DR   STRING; 190304.FN0213; -.
DR   PaxDb; 190304-FN0213; -.
DR   EnsemblBacteria; AAL94419; AAL94419; FN0213.
DR   GeneID; 79783231; -.
DR   KEGG; fnu:FN0213; -.
DR   PATRIC; fig|190304.8.peg.794; -.
DR   eggNOG; COG1778; Bacteria.
DR   HOGENOM; CLU_106694_0_1_0; -.
DR   InParanoid; Q8RGS1; -.
DR   BioCyc; FNUC190304:G1FZS-815-MONOMER; -.
DR   Proteomes; UP000002521; Chromosome.
DR   GO; GO:0019143; F:3-deoxy-manno-octulosonate-8-phosphatase activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050124; F:N-acylneuraminate-9-phosphatase activity; IEA:UniProtKB-EC.
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; 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:0000313|EMBL:AAL94419.1};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR006118-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR006118-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002521}.
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
FT   BINDING         12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
FT   BINDING         103
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
SQ   SEQUENCE   168 AA;  18831 MW;  31A067725C06CD1E CRC64;
     MENIKILVLD VDGTLTNGKI YVDDKDNSFK AFNVKDGFAL VNWLKLGGEV AILTGKKSNI
     VERRAEELGI KYVIQGSKNK TQDLKNLLDR LNITFENTAY MGDDLNDLGV MKNVGLTACP
     KDSVQEILEI SNFISSKNGG DGAVREFLEY IMKNNGMWKK ILEKYSNE
//
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