APHA_RAHSY
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 03-AUG-2022, entry version 50.
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}; OrderedLocusNames=Rahaq_3102;
OS Rahnella sp. (strain Y9602).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 STRING; 741091.Rahaq_3102; -.
DR EnsemblBacteria; ADW74696; ADW74696; Rahaq_3102.
DR KEGG; rah:Rahaq_3102; -.
DR eggNOG; COG3700; Bacteria.
DR HOGENOM; CLU_081496_0_0_6; -.
DR OrthoDB; 1258380at2; -.
DR Proteomes; UP000007257; 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 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..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