APHA_EDWI9
ID APHA_EDWI9 Reviewed; 241 AA.
AC C5BC46;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, 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};
DE Flags: Precursor;
GN Name=aphA {ECO:0000250|UniProtKB:P0AE22}; OrderedLocusNames=NT01EI_3833;
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503;
RN [1] {ECO:0000312|EMBL:ACR70952.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146 {ECO:0000269|Ref.1};
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) 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}.
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DR EMBL; CP001600; ACR70952.1; -; Genomic_DNA.
DR RefSeq; WP_015872984.1; NC_012779.2.
DR AlphaFoldDB; C5BC46; -.
DR SMR; C5BC46; -.
DR STRING; 67780.B6E78_10735; -.
DR EnsemblBacteria; ACR70952; ACR70952; NT01EI_3833.
DR GeneID; 7959874; -.
DR KEGG; eic:NT01EI_3833; -.
DR PATRIC; fig|634503.3.peg.3420; -.
DR HOGENOM; CLU_081496_0_0_6; -.
DR OMA; PEFWEKM; -.
DR OrthoDB; 1258380at2; -.
DR Proteomes; UP000001485; 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 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; Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..241
FT /note="Class B acid phosphatase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000415225"
FT ACT_SITE 72
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0AE22"
FT ACT_SITE 74
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0AE22"
FT BINDING 72
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AE22"
FT BINDING 74
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AE22"
FT BINDING 141..142
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AE22"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AE22"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AE22"
SQ SEQUENCE 241 AA; 26760 MW; 1BD08167680BA319 CRC64;
MFITTKKSLI ALVLATAGLI SSPVSFATET GAQPNLGATL TQLTQQYPIH WISIEQVAES
LKGKAPISVG FDIDDTLLFS SPAFFYGKQK FSPDSNAFLK NQKFWDAVSS SGWDRFSIPK
DSGRALMELH LKRGDHVYFI TGRPMPSNGK EDLTQTLKDD FKIPDNQLNK VIFAGTKQDA
KVEYMQKYHI TIFYGDSDND IQDARKAGAE GIRVLRPLNS TNKPMPKNGA FGEKVIVNSQ
Y