ID   Y028_BUCAI              Reviewed;         272 AA.
AC   P57140; P57141;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   15-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Putative phosphatase BU028/BU029;
DE            EC=3.1.3.-;
GN   OrderedLocusNames=BU028/BU029;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB12756.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BA000003; BAB12755.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BA000003; BAB12756.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; NP_239869.1; NC_002528.1.
DR   RefSeq; NP_239870.1; NC_002528.1.
DR   AlphaFoldDB; P57140; -.
DR   SMR; P57140; -.
DR   STRING; 107806.10038720; -.
DR   EnsemblBacteria; BAB12755; BAB12755; BAB12755.
DR   EnsemblBacteria; BAB12756; BAB12756; BAB12756.
DR   KEGG; buc:BU028; -.
DR   KEGG; buc:BU029; -.
DR   PATRIC; fig|107806.10.peg.40; -.
DR   eggNOG; COG0561; Bacteria.
DR   HOGENOM; CLU_044146_5_2_6; -.
DR   Proteomes; UP000001806; 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..272
FT                   /note="Putative phosphatase BU028/BU029"
FT                   /id="PRO_0000054431"
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   272 AA;  31438 MW;  2B3807FA832C0FDD CRC64;
     MYRIIAVDLD GTLLTSENKI TKYTKEIIQI LIQKKFYFVF ASGRHYIDIM KIKDSLKINI
     FIISSNGSKI YNLDNNLIFS DNLDENIASK LCRIKYSDKE IITQVYQNDQ WYINNNKVEN
     NFCSLLSSLQ YKYFYPDDLN FKNISKIFFT SRNFQKLHIL KRKIINFYGN KVHVNFSIPG
     CLEIVSGDHL KGYGLKLIAN LLGVSLKNCI AFGDGMNDQD MLKVAGKAYI MKNSDPHLKI
     ALPHLEIIES NDNDGVARCL NKIFIENNKE ML