ID   APHA_ENT38              Reviewed;         237 AA.
AC   A4W5G8;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Class B acid phosphatase {ECO:0000250|UniProtKB:P0AE22};
DE            Short=CBAP {ECO:0000250|UniProtKB:P0AE22};
DE            EC=3.1.3.2 {ECO:0000250|UniProtKB:P0AE22, ECO:0000312|EMBL:ABP58948.1};
DE   Flags: Precursor;
GN   Name=aphA {ECO:0000250|UniProtKB:P0AE22}; OrderedLocusNames=Ent638_0259;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
CC   -!- FUNCTION: Dephosphorylates several organic phosphate monoesters. Also
CC       has a phosphotransferase activity catalyzing the transfer of low-energy
CC       phosphate groups from organic phosphate monoesters to free hydroxyl
CC       groups of various organic compounds (By similarity).
CC       {ECO:0000250|UniProtKB:P0AE22}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC         Evidence={ECO:0000250|UniProtKB:P0AE22};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P0AE22};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P0AE22};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0AE22}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P0AE22}.
CC   -!- SIMILARITY: Belongs to the class B bacterial acid phosphatase family.
CC       {ECO:0000250|UniProtKB:P0AE22}.
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DR   EMBL; CP000653; ABP58948.1; -; Genomic_DNA.
DR   RefSeq; WP_011915521.1; NC_009436.1.
DR   AlphaFoldDB; A4W5G8; -.
DR   SMR; A4W5G8; -.
DR   STRING; 399742.Ent638_0259; -.
DR   EnsemblBacteria; ABP58948; ABP58948; Ent638_0259.
DR   KEGG; ent:Ent638_0259; -.
DR   eggNOG; COG3700; Bacteria.
DR   HOGENOM; CLU_081496_0_0_6; -.
DR   OMA; PEFWEKM; -.
DR   OrthoDB; 1258380at2; -.
DR   Proteomes; UP000000230; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd07499; HAD_CBAP; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR005519; Acid_phosphat_B-like.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR010025; HAD-SF_ppase_IIIB_AphA.
DR   InterPro; IPR023214; HAD_sf.
DR   Pfam; PF03767; Acid_phosphat_B; 1.
DR   PIRSF; PIRSF017818; Acid_Ptase_B; 1.
DR   SFLD; SFLDG01127; C1.3:_Acid_Phosphatase_Like; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01672; AphA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Periplasm; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..237
FT                   /note="Class B acid phosphatase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000237561"
FT   ACT_SITE        69
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   ACT_SITE        71
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   BINDING         69
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   BINDING         137..138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   BINDING         192
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
SQ   SEQUENCE   237 AA;  25963 MW;  9D4F8608932A1E42 CRC64;
     MRKITLALSA ACLLFSLNNA VVARASAPTP LYTGTTAAIL AEQAPIHWVS VAQIENSLMG
     RAPMAVGFDI DDTVLFSSPG FWRGKKTFSP ASEEYLKNPE FWEKMNNGWD EFSIPKEVGR
     ALIAMHVKRG DSIYFVTGRS QTKTETVSKT LQGDFAIPSA NMNPVIFAGD KAGQNTKTQW
     LEQKNIKVFY GDSDNDITAA RDVGARGIRV LRASNSTYRP LPMAGAFGEE VIVNSEY