PPAF_PHAVU
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 03-AUG-2022, entry version 130.
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 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 AlphaFoldDB; P80366; -.
DR SMR; P80366; -.
DR STRING; 3885.XP_007131379.1; -.
DR BindingDB; P80366; -.
DR ChEMBL; CHEMBL5670; -.
DR GlyConnect; 306; 12 N-Linked glycans.
DR iPTMnet; P80366; -.
DR PRIDE; 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 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; PTHR22953; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF14008; Metallophos_C; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR SUPFAM; SSF49363; SSF49363; 1.
DR SUPFAM; SSF56300; SSF56300; 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
