ID   PPAF_PHAVU              Reviewed;         459 AA.
AC   P80366; O24319;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   26-NOV-2014, sequence version 3.
DT   24-JAN-2024, entry version 134.
DE   RecName: Full=Fe(3+)-Zn(2+) purple acid phosphatase {ECO:0000303|PubMed:8001554};
DE            Short=PAP {ECO:0000303|PubMed:8001554};
DE            EC=3.1.3.2 {ECO:0000269|PubMed:12054466, ECO:0000269|PubMed:22943065};
DE   AltName: Full=Iron(III)-zinc(II) purple acid phosphatase {ECO:0000305|PubMed:8001554};
DE   Flags: Precursor;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND BLOCKAGE OF N-TERMINUS.
RC   TISSUE=Seed {ECO:0000312|EMBL:CAA04644.1};
RX   PubMed=12054466; DOI=10.1016/s0003-9861(02)00046-2;
RA   Vogel A., Borchers T., Marcus K., Meyer H.E., Krebs B., Spener F.;
RT   "Heterologous expression and characterization of recombinant purple acid
RT   phosphatase from red kidney bean.";
RL   Arch. Biochem. Biophys. 401:164-172(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 28-459.
RC   TISSUE=Seed {ECO:0000303|PubMed:8001554};
RX   PubMed=8001554; DOI=10.1111/j.1432-1033.1994.tb20061.x;
RA   Klabunde T., Stahl B., Suerbaum H., Hahner S., Karas M., Hillenkamp F.,
RA   Krebs B., Witzel H.;
RT   "The amino acid sequence of the red kidney bean Fe(III)-Zn(II) purple acid
RT   phosphatase. Determination of the amino acid sequence by a combination of
RT   matrix-assisted laser desorption/ionization mass spectrometry and automated
RT   Edman sequencing.";
RL   Eur. J. Biochem. 226:369-375(1994).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION AT ASN-108; ASN-136; ASN-170;
RP   ASN-238 AND ASN-423.
RC   TISSUE=Seed;
RX   PubMed=8125089; DOI=10.1111/j.1432-1033.1994.tb18628.x;
RA   Stahl B., Klabunde T., Witzel H., Krebs B., Steup M., Karas M.,
RA   Hillenkamp F.;
RT   "The oligosaccharides of the Fe(III)-Zn(II) purple acid phosphatase of the
RT   red kidney bean. Determination of the structure by a combination of matrix-
RT   assisted laser desorption/ionization mass spectrometry and selective
RT   enzymic degradation.";
RL   Eur. J. Biochem. 220:321-330(1994).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), COFACTOR, SUBUNIT, AND ACTIVE SITE.
RX   PubMed=7770774; DOI=10.1126/science.7770774;
RA   Straeter N., Klabunde T., Tucker P., Witzel H., Krebs B.;
RT   "Crystal structure of a purple acid phosphatase containing a dinuclear
RT   Fe(III)-Zn(II) active site.";
RL   Science 268:1489-1492(1995).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS), COFACTOR, SUBUNIT, GLYCOSYLATION AT
RP   ASN-108; ASN-136; ASN-170; ASN-238 AND ASN-423, DISULFIDE BOND, AND ACTIVE
RP   SITE.
RX   PubMed=8683579; DOI=10.1006/jmbi.1996.0354;
RA   Klabunde T., Straeter N., Froehlich R., Witzel H., Krebs B.;
RT   "Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal
RT   structures.";
RL   J. Mol. Biol. 259:737-748(1996).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 34-459 IN COMPLEX WITH INHIBITOR,
RP   CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, DISULFIDE BOND,
RP   AND GLYCOSYLATION AT ASN-108; ASN-136; ASN-170 AND ASN-423.
RX   PubMed=22943065; DOI=10.1111/cbdd.12001;
RA   Feder D., Hussein W.M., Clayton D.J., Kan M.W., Schenk G., McGeary R.P.,
RA   Guddat L.W.;
RT   "Identification of purple acid phosphatase inhibitors by fragment-based
RT   screening: promising new leads for osteoporosis therapeutics.";
RL   Chem. Biol. Drug Des. 80:665-674(2012).
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:0000269|PubMed:12054466, ECO:0000269|PubMed:22943065};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:22943065,
CC       ECO:0000269|PubMed:7770774, ECO:0000269|PubMed:8683579};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22943065,
CC       ECO:0000269|PubMed:7770774, ECO:0000269|PubMed:8683579};
CC   -!- ACTIVITY REGULATION: Inhibited by compounds CC24201, CC27209, and
CC       MO07123 (PubMed:22943065). Inhibited by the tetraoxoanions molybdate
CC       and phosphate (PubMed:12054466). Not inhibited by EDTA or tartrate
CC       (PubMed:12054466). {ECO:0000269|PubMed:12054466,
CC       ECO:0000269|PubMed:22943065}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.1. {ECO:0000269|PubMed:12054466};
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:22943065,
CC       ECO:0000269|PubMed:7770774, ECO:0000269|PubMed:8683579}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:12054466}.
CC   -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC       acid phosphatase family. {ECO:0000305}.
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DR   EMBL; AJ001270; CAA04644.1; -; mRNA.
DR   PDB; 1KBP; X-ray; 2.65 A; A/B/C/D=28-459.
DR   PDB; 2QFP; X-ray; 2.20 A; A/B/C/D=36-459.
DR   PDB; 2QFR; X-ray; 2.40 A; A/B=36-459.
DR   PDB; 3KBP; X-ray; 3.00 A; A/B/C/D=28-459.
DR   PDB; 4DHL; X-ray; 2.30 A; A/B/C/D=34-459.
DR   PDB; 4DSY; X-ray; 2.30 A; A/B/C/D=34-459.
DR   PDB; 4DT2; X-ray; 2.70 A; A/B/C/D=34-459.
DR   PDB; 4KBP; X-ray; 2.70 A; A/B/C/D=28-459.
DR   PDB; 6G46; X-ray; 2.40 A; A/B/C/D=34-459.
DR   PDB; 6HWR; X-ray; 1.95 A; A/B/C/D=34-459.
DR   PDB; 6OF5; X-ray; 2.30 A; A/B/C/D=34-459.
DR   PDB; 6OFD; X-ray; 2.20 A; A/B/C/D=1-459.
DR   PDB; 6PY9; X-ray; 2.20 A; A/B/C/D=1-459.
DR   PDB; 6VJ7; X-ray; 2.60 A; A/B/C/D=34-459.
DR   PDB; 8BRN; X-ray; 2.00 A; A/B/C/D=32-459.
DR   PDBsum; 1KBP; -.
DR   PDBsum; 2QFP; -.
DR   PDBsum; 2QFR; -.
DR   PDBsum; 3KBP; -.
DR   PDBsum; 4DHL; -.
DR   PDBsum; 4DSY; -.
DR   PDBsum; 4DT2; -.
DR   PDBsum; 4KBP; -.
DR   PDBsum; 6G46; -.
DR   PDBsum; 6HWR; -.
DR   PDBsum; 6OF5; -.
DR   PDBsum; 6OFD; -.
DR   PDBsum; 6PY9; -.
DR   PDBsum; 6VJ7; -.
DR   PDBsum; 8BRN; -.
DR   AlphaFoldDB; P80366; -.
DR   SMR; P80366; -.
DR   BindingDB; P80366; -.
DR   ChEMBL; CHEMBL5670; -.
DR   GlyConnect; 306; 12 N-Linked glycans.
DR   iPTMnet; P80366; -.
DR   eggNOG; KOG1378; Eukaryota.
DR   BRENDA; 3.1.3.2; 4746.
DR   SABIO-RK; P80366; -.
DR   EvolutionaryTrace; P80366; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003993; F:acid phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0008199; F:ferric iron binding; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
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; IPR004843; Calcineurin-like_PHP_ApaH.
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:SF86; PURPLE ACID PHOSPHATASE 10; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF14008; Metallophos_C; 1.
DR   Pfam; PF16656; Pur_ac_phosph_N; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF49363; Purple acid phosphatase, N-terminal domain; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hydrolase; Iron; Metal-binding; Secreted; Signal; Zinc.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:12054466"
FT   CHAIN           23..459
FT                   /note="Fe(3+)-Zn(2+) purple acid phosphatase"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:12054466"
FT                   /id="PRO_0000114474"
FT   ACT_SITE        323
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000303|PubMed:7770774,
FT                   ECO:0000303|PubMed:8683579"
FT   BINDING         162
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000269|PubMed:22943065,
FT                   ECO:0000269|PubMed:8683579"
FT   BINDING         191
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000269|PubMed:22943065,
FT                   ECO:0000269|PubMed:8683579"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:22943065,
FT                   ECO:0000269|PubMed:8683579"
FT   BINDING         194
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000269|PubMed:22943065,
FT                   ECO:0000269|PubMed:8683579"
FT   BINDING         228
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:22943065,
FT                   ECO:0000269|PubMed:8683579"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:22943065,
FT                   ECO:0000269|PubMed:8683579"
FT   BINDING         350
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:22943065,
FT                   ECO:0000269|PubMed:8683579"
FT   BINDING         352
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000269|PubMed:22943065,
FT                   ECO:0000269|PubMed:8683579"
FT   MOD_RES         23
FT                   /note="Blocked amino end (Gly)"
FT                   /evidence="ECO:0000269|PubMed:12054466"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine; partial"
FT                   /evidence="ECO:0000269|PubMed:22943065,
FT                   ECO:0000269|PubMed:8125089, ECO:0000269|PubMed:8683579"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22943065,
FT                   ECO:0000269|PubMed:8125089, ECO:0000269|PubMed:8683579"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22943065,
FT                   ECO:0000269|PubMed:8125089, ECO:0000269|PubMed:8683579"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8125089,
FT                   ECO:0000269|PubMed:8683579"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22943065,
FT                   ECO:0000269|PubMed:8125089, ECO:0000269|PubMed:8683579"
FT   DISULFID        372
FT                   /note="Interchain"
FT                   /evidence="ECO:0000269|PubMed:22943065,
FT                   ECO:0000269|PubMed:8683579"
FT   CONFLICT        280..281
FT                   /note="YS -> HI (in Ref. 2; AA sequence)"
FT   CONFLICT        369
FT                   /note="N -> D (in Ref. 2; AA sequence)"
FT   HELIX           43..45
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          55..61
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          63..67
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          69..78
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          84..88
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   TURN            89..91
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          113..119
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          127..132
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:2QFP"
FT   STRAND          139..144
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          155..160
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          164..166
FT                   /evidence="ECO:0007829|PDB:6VJ7"
FT   HELIX           167..177
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          184..188
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   HELIX           195..197
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   HELIX           199..201
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   HELIX           204..217
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          222..224
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   HELIX           228..231
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   HELIX           235..237
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   HELIX           244..249
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   HELIX           254..257
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          264..269
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          272..276
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   HELIX           288..299
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   TURN            302..304
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          307..311
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   TURN            322..327
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   HELIX           328..340
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          345..348
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          350..357
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          359..361
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          367..369
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          382..386
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   TURN            391..393
FT                   /evidence="ECO:0007829|PDB:1KBP"
FT   STRAND          407..411
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          415..421
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          423..433
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   STRAND          442..448
FT                   /evidence="ECO:0007829|PDB:6HWR"
FT   TURN            450..452
FT                   /evidence="ECO:0007829|PDB:6HWR"
SQ   SEQUENCE   459 AA;  52857 MW;  CC379B7C1AE4D21A CRC64;
     MGVVKGLLAL ALVLNVVVVS NGGKSSNFVR KTNKNRDMPL DSDVFRVPPG YNAPQQVHIT
     QGDLVGRAMI ISWVTMDEPG SSAVRYWSEK NGRKRIAKGK MSTYRFFNYS SGFIHHTTIR
     KLKYNTKYYY EVGLRNTTRR FSFITPPQTG LDVPYTFGLI GDLGQSFDSN TTLSHYELSP
     KKGQTVLFVG DLSYADRYPN HDNVRWDTWG RFTERSVAYQ PWIWTAGNHE IEFAPEINET
     EPFKPFSYRY HVPYEASQST SPFWYSIKRA SAHIIVLSSY SAYGRGTPQY TWLKKELRKV
     KRSETPWLIV LMHSPLYNSY NHHFMEGEAM RTKFEAWFVK YKVDVVFAGH VHAYERSERV
     SNIAYKITNG LCTPVKDQSA PVYITIGDAG NYGVIDSNMI QPQPEYSAFR EASFGHGMFD
     IKNRTHAHFS WNRNQDGVAV EADSVWFFNR HWYPVDDST
//