ID   Y030_BUCBP              Reviewed;         267 AA.
AC   Q89B25;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Putative phosphatase bbp_030;
DE            EC=3.1.3.-;
GN   OrderedLocusNames=bbp_030;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO26773.1; -; Genomic_DNA.
DR   RefSeq; WP_011091174.1; NC_004545.1.
DR   AlphaFoldDB; Q89B25; -.
DR   SMR; Q89B25; -.
DR   STRING; 224915.bbp_030; -.
DR   EnsemblBacteria; AAO26773; AAO26773; bbp_030.
DR   GeneID; 56470574; -.
DR   KEGG; bab:bbp_030; -.
DR   eggNOG; COG0561; Bacteria.
DR   HOGENOM; CLU_044146_5_2_6; -.
DR   OMA; CCAERGI; -.
DR   OrthoDB; 1374424at2; -.
DR   Proteomes; UP000000601; 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; Reference proteome.
FT   CHAIN           1..267
FT                   /note="Putative phosphatase bbp_030"
FT                   /id="PRO_0000054433"
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   267 AA;  30904 MW;  DC729528834038C0 CRC64;
     MYYIVASDLD GTLLSPQFYL TEYTKKIIKR LVNKGIYFVI ATGRHYNEAK EIQKMLNVPV
     FLITSNGARI YDLNKKLIYS CDIEQKVVKE LLQKCLLNHD ILIQLYSHNN WYVSNNNYSA
     SSLYVSFSFR SKIFEFKTII KKKISKIFFT CKNVKKLLCL EKYIISHWGK YVNVSFSFLN
     CLEIMSKTVS KGNSLQLIAN MLGLSIKNCI SFGDGMNDKE MLDMSGKGCM MDNSHYLLKK
     SLPNLEIIGS NKFDSVAMYL NKIYFKK