KDSC_HAEIN
ID KDSC_HAEIN Reviewed; 180 AA.
AC P45314;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC;
DE EC=3.1.3.45 {ECO:0000269|PubMed:12639950};
DE AltName: Full=KDO 8-P phosphatase;
GN OrderedLocusNames=HI_1679;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP FUNCTION AS A KDO 8-P PHOSPHATASE, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=12639950; DOI=10.1074/jbc.m301983200;
RA Wu J., Woodard R.W.;
RT "Escherichia coli YrbI is 3-deoxy-D-manno-octulosonate 8-phosphate
RT phosphatase.";
RL J. Biol. Chem. 278:18117-18123(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH DIVALENT METALS,
RP SUBUNIT, AND METAL-BINDING.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=11835514; DOI=10.1002/prot.10057;
RA Parsons J.F., Lim K., Tempczyk A., Krajewski W., Eisenstein E.,
RA Herzberg O.;
RT "From structure to function: YrbI from Haemophilus influenzae (HI1679) is a
RT phosphatase.";
RL Proteins 46:393-404(2002).
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:0000269|PubMed:12639950}.
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:0000269|PubMed:12639950};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:12639950};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11835514}.
CC -!- MISCELLANEOUS: Cobalt was used in the crystallography experiment but
CC magnesium is likely to be the physiological metal.
CC -!- SIMILARITY: Belongs to the KdsC family. {ECO:0000305}.
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DR EMBL; L42023; AAC23325.1; -; Genomic_DNA.
DR PIR; G64174; G64174.
DR RefSeq; NP_439821.1; NC_000907.1.
DR RefSeq; WP_005665007.1; NC_000907.1.
DR PDB; 1J8D; X-ray; 2.30 A; A/B/C/D=1-180.
DR PDB; 1K1E; X-ray; 1.67 A; A/B/C/D/E/F/G/H/I/J/K/L=1-180.
DR PDB; 4HGP; X-ray; 1.80 A; A=1-180.
DR PDBsum; 1J8D; -.
DR PDBsum; 1K1E; -.
DR PDBsum; 4HGP; -.
DR AlphaFoldDB; P45314; -.
DR SMR; P45314; -.
DR STRING; 71421.HI_1679; -.
DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR EnsemblBacteria; AAC23325; AAC23325; HI_1679.
DR KEGG; hin:HI_1679; -.
DR PATRIC; fig|71421.8.peg.1758; -.
DR eggNOG; COG1778; Bacteria.
DR HOGENOM; CLU_106694_1_0_6; -.
DR OMA; VFMGVEN; -.
DR PhylomeDB; P45314; -.
DR BioCyc; HINF71421:G1GJ1-1695-MON; -.
DR BRENDA; 3.1.3.45; 2529.
DR EvolutionaryTrace; P45314; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0019143; F:3-deoxy-manno-octulosonate-8-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; -; 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 PIRSF; PIRSF006118; KDO8-P_Ptase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
DR TIGRFAMs; TIGR01670; KdsC-phosphatas; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Lipopolysaccharide biosynthesis; Magnesium;
KW Metal-binding; Reference proteome.
FT CHAIN 1..180
FT /note="3-deoxy-D-manno-octulosonate 8-phosphate phosphatase
FT KdsC"
FT /id="PRO_0000201703"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:11835514"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:11835514"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 37..41
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P67653"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:11835514"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:1K1E"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:1K1E"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:1K1E"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:1K1E"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:1K1E"
FT HELIX 38..49
FT /evidence="ECO:0007829|PDB:1K1E"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:1K1E"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:1K1E"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1K1E"
FT HELIX 84..95
FT /evidence="ECO:0007829|PDB:1K1E"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1K1E"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:1K1E"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1K1E"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:1K1E"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:1K1E"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:1K1E"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:1K1E"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:1K1E"
FT HELIX 147..158
FT /evidence="ECO:0007829|PDB:1K1E"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:1K1E"
FT HELIX 168..174
FT /evidence="ECO:0007829|PDB:1K1E"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1K1E"
SQ SEQUENCE 180 AA; 19432 MW; 23CD435E4E83A095 CRC64;
MQQKLENIKF VITDVDGVLT DGQLHYDANG EAIKSFHVRD GLGIKMLMDA DIQVAVLSGR
DSPILRRRIA DLGIKLFFLG KLEKETACFD LMKQAGVTAE QTAYIGDDSV DLPAFAACGT
SFAVADAPIY VKNAVDHVLS THGGKGAFRE MSDMILQAQG KSSVFDTAQG FLKSVKSMGQ
