ID   PHOA_ASPNG              Reviewed;         417 AA.
AC   P34724;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Acid phosphatase;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=phoA;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=NRRL 3135 / Van Tieghem / Ficuum;
RX   PubMed=7945393; DOI=10.1006/bbrc.1994.2426;
RA   Ehrlich K.C., Montalbano B.G., Mullaney E.J., Dischinger H.C. Jr.,
RA   Ullah A.H.J.;
RT   "An acid phosphatase from Aspergillus ficuum has homology to Penicillium
RT   chrysogenum PhoA.";
RL   Biochem. Biophys. Res. Commun. 204:63-68(1994).
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: The N-terminus is blocked.
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DR   EMBL; L20566; AAA62393.1; -; Genomic_DNA.
DR   AlphaFoldDB; P34724; -.
DR   STRING; 5061.CADANGAP00010874; -.
DR   VEuPathDB; FungiDB:An14g01550; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1115461; -.
DR   VEuPathDB; FungiDB:ATCC64974_1420; -.
DR   VEuPathDB; FungiDB:M747DRAFT_271610; -.
DR   eggNOG; ENOG502QSRP; Eukaryota.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.720.10; -; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR007312; Phosphoesterase.
DR   PANTHER; PTHR31956; PTHR31956; 1.
DR   Pfam; PF04185; Phosphoesterase; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..417
FT                   /note="Acid phosphatase"
FT                   /id="PRO_0000023978"
FT   ACT_SITE        216
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        209
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        218
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        383
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   417 AA;  46736 MW;  896FD2AF541C69C8 CRC64;
     MFTKQSLVTL LGGLSLAVAQ TTTEGYPSLA EIRAAQATVQ PYSPVSNVKG LTFNRFVNIW
     LENTDFDAAA ATEHLPVLAK KGLLLNNFWA VTHPSEPNYC RHLPLGDTFG MDNDDFHQIP
     SNVSTIADLF DTKNIAWGEY QEGLPYPGYQ GYRYPESGAN DYVRNRNPLI LFDSVTEDAL
     RLRQIKNFSS FYDDLENHRL PQYMFITPNM TNDGHDTNIT FSGDWTWGFL SELLENDYFT
     KDTLIMLTFD ETGTYEIGNN IYTFLLGGAV PDDLLGTKDD TFYTHYSVIA SLSTNWGLPS
     LGRWDCGANL FSWLAKKTGY VNYEVDTSNL YMNETHWGPL SDDDYSEYYA GWPVPTTDAS
     CSAGNGILST VKKTYEGLTA TFNYTTPFPY DSRSGNNVGV KYSRTLKNGK VESGTSE