ID   APHA_RAHSY              Reviewed;         237 AA.
AC   E8XMF0;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 2.
DT   02-SEP-2026, entry version 61.
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:ADW74696.1};
DE   Flags: Precursor;
GN   Name=aphA {ECO:0000250|UniProtKB:P0AE22};
GN   OrderedLocusNames=Rahaq_3102;
OS   Rahnella sp. (strain Y9602).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Yersiniaceae; Rahnella.
OX   NCBI_TaxID=2703885;
RN   [1] {ECO:0000312|EMBL:ADW74696.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y9602 {ECO:0000312|EMBL:ADW74696.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Ovchinnikova G., Pagani I., Sobecky P.A., Martinez R.J.,
RA   Woyke T.;
RT   "Complete sequence of chromosome of Rahnella sp. Y9602.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ADW74696.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP002505; ADW74696.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_015690236.1; NC_015061.1.
DR   AlphaFoldDB; E8XMF0; -.
DR   SMR; E8XMF0; -.
DR   GeneID; 305417747; -.
DR   KEGG; rah:Rahaq_3102; -.
DR   eggNOG; COG3700; Bacteria.
DR   HOGENOM; CLU_081496_0_0_6; -.
DR   OrthoDB; 2234478at2; -.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0042597; C:periplasmic space; ISS:UniProtKB.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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   NCBIfam; TIGR01672; AphA; 1.
DR   Pfam; PF03767; Acid_phosphat_B; 1.
DR   PIRSF; PIRSF017818; Acid_Ptase_B; 1.
DR   SFLD; SFLDG01127; C1.3:_Acid_Phosphatase_Like; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Periplasm; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..237
FT                   /note="Class B acid phosphatase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000703176"
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;  26216 MW;  8F9565C278739505 CRC64;
     MRKTPLALSA VFLLLSLNQS AFAKEPAPAP LWPGVNVAQL AQQSPVHWVS VAQIENSLNG
     RPPIAVGFDI DDTVLFSSPG FYRGQVEFSP GKQDYLKNPK FWEKMNNGWD DFSMPKEVAK
     SLIAMHLKRG DSIYFVTGRS ETKTETVTKT LQNDFQIPQD KVNAVIFAGD KAGQNTKTQW
     LKDKQIKVFY GDSDNDITAA QSVSARGIRV LRASNSSYKP LPQAGAFGEE VIVNSEY
//