PPAF1_IPOBA
ID PPAF1_IPOBA Reviewed; 473 AA.
AC Q9SE00;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Purple acid phosphatase 1;
DE EC=3.1.3.2;
DE AltName: Full=Manganese(II) purple acid phosphatase 1;
DE Flags: Precursor;
GN Name=PAP1;
OS Ipomoea batatas (Sweet potato) (Convolvulus batatas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX NCBI_TaxID=4120;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, COFACTOR, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Golden;
RX PubMed=10510276; DOI=10.1006/abbi.1999.1407;
RA Schenk G., Ge Y., Carrington L.E., Wynne C.J., Searle I.R., Carroll B.J.,
RA Hamilton S., de Jersey J.;
RT "Binuclear metal centers in plant purple acid phosphatases: Fe-Mn in sweet
RT potato and Fe-Zn in soybean.";
RL Arch. Biochem. Biophys. 370:183-189(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-464 IN COMPLEX WITH SUBSTRATE
RP AND COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15625111; DOI=10.1073/pnas.0407239102;
RA Schenk G., Gahan L.R., Carrington L.E., Mitic N., Valizadeh M.,
RA Hamilton S.E., de Jersey J., Guddat L.W.;
RT "Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet
RT potato purple acid phosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:273-278(2005).
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:10510276};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10510276};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:10510276};
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:10510276};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10510276};
CC Note=Binds 1 Mn(2+) ion per subunit. Can also use Zn(2+), Cu(2+) and
CC Mg(2+) ions. {ECO:0000269|PubMed:10510276};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=560 nm {ECO:0000269|PubMed:10510276,
CC ECO:0000269|PubMed:15625111};
CC Kinetic parameters:
CC KM=95 uM for p-NPP (at pH 4.9 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:10510276, ECO:0000269|PubMed:15625111};
CC KM=120 uM for ATP (at pH 4.9 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:10510276, ECO:0000269|PubMed:15625111};
CC KM=180 uM for ADP (at pH 4.9 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:10510276, ECO:0000269|PubMed:15625111};
CC KM=360 uM for AMP (at pH 4.9 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:10510276, ECO:0000269|PubMed:15625111};
CC KM=75 uM for pyrophosphate (at pH 4.9 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:10510276, ECO:0000269|PubMed:15625111};
CC KM=490 uM for beta-glycerophosphate (at pH 4.9 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:10510276, ECO:0000269|PubMed:15625111};
CC KM=44 uM for 4-nitrophenol phosphate (at pH 3.5)
CC {ECO:0000269|PubMed:10510276, ECO:0000269|PubMed:15625111};
CC KM=68 uM for 4-nitrophenol phosphate (at pH 4)
CC {ECO:0000269|PubMed:10510276, ECO:0000269|PubMed:15625111};
CC KM=68 uM for 4-nitrophenol phosphate (at pH 4.5)
CC {ECO:0000269|PubMed:10510276, ECO:0000269|PubMed:15625111};
CC KM=93 uM for 4-nitrophenol phosphate (at pH 5)
CC {ECO:0000269|PubMed:10510276, ECO:0000269|PubMed:15625111};
CC KM=330 uM for 4-nitrophenol phosphate (at pH 6)
CC {ECO:0000269|PubMed:10510276, ECO:0000269|PubMed:15625111};
CC KM=930 uM for 4-nitrophenol phosphate (at pH 6.5)
CC {ECO:0000269|PubMed:10510276, ECO:0000269|PubMed:15625111};
CC KM=1800 uM for 4-nitrophenol phosphate (at pH 7)
CC {ECO:0000269|PubMed:10510276, ECO:0000269|PubMed:15625111};
CC KM=5000 uM for 4-nitrophenol phosphate (at pH 8)
CC {ECO:0000269|PubMed:10510276, ECO:0000269|PubMed:15625111};
CC pH dependence:
CC Optimum pH is 4.5. {ECO:0000269|PubMed:10510276,
CC ECO:0000269|PubMed:15625111};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC acid phosphatase family. {ECO:0000305}.
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DR EMBL; AF200825; AAF19821.1; -; mRNA.
DR PIR; A59200; A59200.
DR PDB; 1XZW; X-ray; 2.50 A; A/B=39-464.
DR PDBsum; 1XZW; -.
DR AlphaFoldDB; Q9SE00; -.
DR SMR; Q9SE00; -.
DR PRIDE; Q9SE00; -.
DR BioCyc; MetaCyc:MON-15153; -.
DR BRENDA; 3.1.3.2; 2773.
DR SABIO-RK; Q9SE00; -.
DR EvolutionaryTrace; Q9SE00; -.
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:UniProtKB-KW.
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; Disulfide bond; Glycoprotein; Hydrolase; Iron; Metal-binding;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..473
FT /note="Purple acid phosphatase 1"
FT /id="PRO_5000057351"
FT ACT_SITE 333
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 204
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 360..362
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 362
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 382
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:1XZW"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:1XZW"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1XZW"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:1XZW"
FT HELIX 177..188
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:1XZW"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:1XZW"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1XZW"
FT HELIX 214..227
FT /evidence="ECO:0007829|PDB:1XZW"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1XZW"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:1XZW"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:1XZW"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:1XZW"
FT HELIX 298..309
FT /evidence="ECO:0007829|PDB:1XZW"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:1XZW"
FT TURN 332..337
FT /evidence="ECO:0007829|PDB:1XZW"
FT HELIX 338..350
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 360..367
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 392..396
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 417..421
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 425..431
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 433..443
FT /evidence="ECO:0007829|PDB:1XZW"
FT STRAND 452..458
FT /evidence="ECO:0007829|PDB:1XZW"
SQ SEQUENCE 473 AA; 53815 MW; BAE4B807DADD95A7 CRC64;
MRLVVVGLWC LILGLILNPT KFCDAGVTSS YVRKSLSALP NAEDVDMPWD SDVFAVPSGY
NAPQQVHITQ GDYEGRGVII SWTTPYDKAG ANKVVYWSEN SKSQKRAMGT VVTYKYYNYT
SAFIHHCTIK DLEYDTKYYY RLGFGDAKRQ FWFVTPPKPG PDVPYVFGLI GDIGQTHDSN
TTLTHYEQNS AKGQAVLFMG DLSYSNRWPN HDNNRWDTWG RFSERSVAYQ PWIWTAGNHE
IDYAPDIGEY QPFVPFTNRY PTPHEASGSG DPLWYAIKRA SAHIIVLSSY SGFVKYSPQY
KWFTSELEKV NRSETPWLIV LVHAPLYNSY EAHYMEGEAM RAIFEPYFVY YKVDIVFSGH
VHSYERSERV SNVAYNIVNA KCTPVSDESA PVYITIGDGG NSEGLASEMT QPQPSYSAFR
EASFGHGIFD IKNRTHAHFS WHRNQDGASV EADSLWLLNR YWASEDASSM SAM
