ID   Y029_BUCAP              Reviewed;         274 AA.
AC   Q8KA73;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Putative phosphatase BUsg_029;
DE            EC=3.1.3.-;
GN   OrderedLocusNames=BUsg_029;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67600.1; -; Genomic_DNA.
DR   RefSeq; WP_011053566.1; NC_004061.1.
DR   AlphaFoldDB; Q8KA73; -.
DR   SMR; Q8KA73; -.
DR   STRING; 198804.BUsg_029; -.
DR   PRIDE; Q8KA73; -.
DR   EnsemblBacteria; AAM67600; AAM67600; BUsg_029.
DR   KEGG; bas:BUsg_029; -.
DR   eggNOG; COG0561; Bacteria.
DR   HOGENOM; CLU_044146_5_2_6; -.
DR   OMA; CCAERGI; -.
DR   OrthoDB; 1374424at2; -.
DR   Proteomes; UP000000416; 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.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..274
FT                   /note="Putative phosphatase BUsg_029"
FT                   /id="PRO_0000054432"
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         9
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         42..43
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   274 AA;  31349 MW;  DC891E3695E183D7 CRC64;
     MYRIIAADLD GTLLSPENKI TKYTEKIIKF LIEKGFYFVF ASGRHYIDIM KIRDTLNIKV
     FMITSNGAQV YDLNNVLIFE NHLDEEIALK LCKMKYLDAD IITQVYRNNQ WYINNNKIDN
     NFCPTLSSLR YKYFCPDVFN FKKVSKVFFT SHNLKKLHTL QKDIISFLGN RVNVHFSVPG
     CLEVVSGEVS KGYGLKLISN ILGISLKECI TFGDGMNDQD MLSISGKACI MENADSSLKK
     NLPYAEVIGS NKNDGVAVFL NKNFIKNNKF IKCF