Y597_HAEIN
ID Y597_HAEIN Reviewed; 272 AA.
AC P44771;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Putative phosphatase HI_0597;
DE EC=3.1.3.-;
GN OrderedLocusNames=HI_0597;
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).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC22254.1; -; Genomic_DNA.
DR PIR; D64155; D64155.
DR RefSeq; NP_438754.1; NC_000907.1.
DR RefSeq; WP_005694570.1; NC_000907.1.
DR AlphaFoldDB; P44771; -.
DR SMR; P44771; -.
DR STRING; 71421.HI_0597; -.
DR DNASU; 950123; -.
DR EnsemblBacteria; AAC22254; AAC22254; HI_0597.
DR KEGG; hin:HI_0597; -.
DR PATRIC; fig|71421.8.peg.618; -.
DR eggNOG; COG0561; Bacteria.
DR HOGENOM; CLU_044146_5_2_6; -.
DR OMA; CCAERGI; -.
DR PhylomeDB; P44771; -.
DR BioCyc; HINF71421:G1GJ1-607-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016791; F:phosphatase activity; IEA:UniProt.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR000150; Cof.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR00099; Cof-subfamily; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR PROSITE; PS01228; COF_1; 1.
DR PROSITE; PS01229; COF_2; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..272
FT /note="Putative phosphatase HI_0597"
FT /id="PRO_0000054428"
FT ACT_SITE 11
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 45..46
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
SQ SEQUENCE 272 AA; 30523 MW; 5BC412A9B2892A52 CRC64;
MNLPFRAMVS DLDGTLLTPE HLVGDLTIDT LRALEQKGVD IILATGRNHT DVSSILGKIG
AERAVMITSN GARVRDLQGN LLYSNSLPEE LVLELYKTPF DTSKVCMNSY QDEGWFTNKD
IPAMRQFHKE SGFDYNVVDF SKHHGRGTEK VFFIGKTPED LVEVETYLRD KFGDVTTIVY
SALACLEVMN KNVSKGDALK HLLESREYEL KDCIAFGDGM NDVEMLSWAG KGCIMKDADI
RLKMACPELE VIGSNKEESV ARYLRTQFGL DY
