ID   PPA_ASPFI               Reviewed;         614 AA.
AC   Q12546;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Acid phosphatase;
DE            EC=3.1.3.2;
DE   AltName: Full=APase6;
DE   AltName: Full=pH 6-optimum acid phosphatase;
DE   Flags: Precursor;
GN   Name=aphA;
OS   Aspergillus ficuum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 66876 / DSM 932 / SRRC 265 / NRRL 3135;
RX   PubMed=7557398; DOI=10.1016/0378-1119(95)00298-k;
RA   Mullaney E.J., Daly C.B., Ehrlich K.C., Ullah A.H.J.;
RT   "The Aspergillus niger (ficuum) aphA gene encodes a pH 6.0-optimum acid
RT   phosphatase.";
RL   Gene 162:117-121(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 23-605.
RC   STRAIN=ATCC 66876 / DSM 932 / SRRC 265 / NRRL 3135;
RX   PubMed=8074654; DOI=10.1006/bbrc.1994.2166;
RA   Ullah A.H.J., Mullaney E.M., Dischinger H.C. Jr.;
RT   "The complete primary structure elucidation of Aspergillus ficuum (niger),
RT   pH 6.0, optimum acid phosphatase by Edman degradation.";
RL   Biochem. Biophys. Res. Commun. 203:182-189(1994).
RN   [3]
RP   PROTEIN SEQUENCE OF 23-56, AND CHARACTERIZATION.
RC   STRAIN=ATCC 66876 / DSM 932 / SRRC 265 / NRRL 3135;
RX   PubMed=3375203; DOI=10.1080/00327488808062512;
RA   Ullah A.H.J., Cummins B.J.;
RT   "Aspergillus ficuum extracellular pH 6.0 optimum acid phosphatase:
RT   purification, N-terminal amino acid sequence, and biochemical
RT   characterization.";
RL   Prep. Biochem. 18:37-65(1988).
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   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000305};
CC   -!- ACTIVITY REGULATION: Competitively inhibited by phosphomycin and
CC       inorganic orthophosphate.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6. Inactive above pH 6.7.;
CC       Temperature dependence:
CC         Optimum temperature is 63 degrees Celsius.;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Glycosylated; probably with N-linked high-mannose
CC       oligosaccharides.
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DR   EMBL; U18553; AAA91632.1; -; Genomic_DNA.
DR   PIR; JC2545; JC2545.
DR   AlphaFoldDB; Q12546; -.
DR   SMR; Q12546; -.
DR   GlyCosmos; Q12546; 13 sites, No reported glycans.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd00839; MPP_PAPs; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR   InterPro; IPR014390; Acid_Pase_Asper.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041792; MPP_PAP.
DR   InterPro; IPR039331; PPA-like.
DR   InterPro; IPR008963; Purple_acid_Pase-like_N.
DR   InterPro; IPR015914; Purple_acid_Pase_N.
DR   InterPro; IPR025733; Purple_acid_PPase_C_dom.
DR   PANTHER; PTHR22953; ACID PHOSPHATASE RELATED; 1.
DR   PANTHER; PTHR22953:SF159; PURPLE ACID PHOSPHATASE; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF14008; Metallophos_C; 1.
DR   Pfam; PF16656; Pur_ac_phosph_N; 1.
DR   PIRSF; PIRSF000900; Acid_Ptase_Asper; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF49363; Purple acid phosphatase, N-terminal domain; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Glycoprotein; Hydrolase; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:3375203,
FT                   ECO:0000269|PubMed:8074654"
FT   CHAIN           23..605
FT                   /note="Acid phosphatase"
FT                   /id="PRO_0000023997"
FT   PROPEP          606..614
FT                   /id="PRO_0000023998"
FT   DOMAIN          80..176
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
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        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        408
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        512
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        523
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        559
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        578
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   614 AA;  67211 MW;  7016738F63C62EBE CRC64;
     MKGTAASALL VALSATAAQA RPVVDERFPY TGPAVPIGDW VDPTINGNGK GFPRLVEPPA
     VKPATANPRN NVNVISLSYI PKGMHIHYQT PFGLGQLPAV RWGKDPRNLN STAQGYSHTY
     DRTPSCSQVK AVTQCSQFFH EVSIDGLEPD TTYYYQIPAA NGTTQSEVLS FKTSRPAGHP
     GSFSVAVLND MGYTNAHGTH KQLVKAATEG TAFAWHGGDL SYADDWYSGI LACADDWPVC
     YNGTSSTLPG GGPLPEEYKK PLPAGEIPDQ GGPQGGDMSV LYESNWDLWQ QWLNNVTLKI
     PYMVLPGNHE ASCAEFDGPH NILTAYLNDD IANGTAPTDN LTYYSCPPSQ RNFTAYQHRF
     RMPGPETGGV GNFWYSFDYG LAHFVSIDGE TDFANSPEWN FAEDVTGNET LPSESETFIT
     DSGPFGNVNG SVHETKSYEQ WHWLQQDLAK VDRSKTPWVI VMSHRPMYSS AYSSYQLHVR
     EAFEGLLLKY GVDAYLSGHI HWYERLYPLG ANGTIDTAAI VNNNTYYAHN GKSITHIING
     MAGNIESHSE FSDGEGLTNI TALLDKVHYG FSKLTIFNET ALKWELIRGD DGTVGDSLTL
     LKPSHVAGGK KLHS
//