ID PPAF_SOYBN Reviewed; 464 AA. AC Q09131; Q9SE01; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 2. DT 24-JAN-2024, entry version 99. DE RecName: Full=Purple acid phosphatase; DE EC=3.1.3.2; DE AltName: Full=Zinc(II) purple acid phosphatase; DE Flags: Precursor; GN Name=PAP {ECO:0000312|EMBL:AAF19820.1}; OS Glycine max (Soybean) (Glycine hispida). 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; Glycine; OC Glycine subgen. Soja. OX NCBI_TaxID=3847; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF19820.1} RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, COFACTOR, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=cv. Provar; 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 PROTEIN SEQUENCE OF 31-47, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=16668896; DOI=10.1104/pp.99.2.391; RA Lebansky B.R., McKnight T.D., Griffing L.R.; RT "Purification and characterization of a secreted purple phosphatase from RT soybean suspension cultures."; RL Plant Physiol. 99:391-395(1992). 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, ECO:0000269|PubMed:16668896}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Evidence={ECO:0000269|PubMed:10510276}; CC Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:10510276}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 zinc ion per subunit. Can also use manganese, copper and CC magnesium ions.; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Absorption: CC Abs(max)=550 nm {ECO:0000269|PubMed:10510276}; CC Kinetic parameters: CC KM=8 uM for p-NPP (at pH 5.5 and 25 degrees Celsius) CC {ECO:0000269|PubMed:10510276}; CC KM=5 uM for ATP (at pH 5.5 and 25 degrees Celsius) CC {ECO:0000269|PubMed:10510276}; CC KM=6 uM for ADP (at pH 5.5 and 25 degrees Celsius) CC {ECO:0000269|PubMed:10510276}; CC KM=9 uM for AMP (at pH 5.5 and 25 degrees Celsius) CC {ECO:0000269|PubMed:10510276}; CC KM=9 uM for pyrophosphate (at pH 5.5 and 25 degrees Celsius) CC {ECO:0000269|PubMed:10510276}; CC KM=30 uM for beta-glycerophosphate (at pH 5.5 and 25 degrees Celsius) CC {ECO:0000269|PubMed:10510276}; CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P80366, CC ECO:0000269|PubMed:16668896}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16668896}. CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple CC acid phosphatase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF200824; AAF19820.1; -; mRNA. DR PIR; B59200; B59200. DR AlphaFoldDB; Q09131; -. DR SMR; Q09131; -. DR STRING; 3847.Q09131; -. DR GlyCosmos; Q09131; 6 sites, No reported glycans. DR PaxDb; 3847-GLYMA09G36360-1; -. DR eggNOG; KOG1378; Eukaryota. DR InParanoid; Q09131; -. DR BioCyc; MetaCyc:MONOMER-15155; -. DR SABIO-RK; Q09131; -. DR Proteomes; UP000008827; Unplaced. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0003993; F:acid phosphatase activity; IDA:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB. DR GO; GO:0046872; F:metal 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 Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; Iron; KW Metal-binding; Reference proteome; Secreted; Signal; Zinc. FT SIGNAL 1..30 FT /evidence="ECO:0000269|PubMed:16668896" FT CHAIN 31..464 FT /note="Purple acid phosphatase" FT /evidence="ECO:0000269|PubMed:16668896" FT /id="PRO_0000043380" FT ACT_SITE 323 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P80366" FT BINDING 162 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250|UniProtKB:P80366" FT BINDING 191 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250|UniProtKB:P80366" FT BINDING 191 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P80366" FT BINDING 194 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250|UniProtKB:P80366" FT BINDING 228 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 228 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P80366" FT BINDING 313 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P80366" FT BINDING 350..352 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 350 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P80366" FT BINDING 352 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250|UniProtKB:P80366" FT CARBOHYD 108 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 136 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 170 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 301 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 398 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 423 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 372 FT /note="Interchain" FT /evidence="ECO:0000250|UniProtKB:P80366" FT CONFLICT 35 FT /note="T -> A (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 47 FT /note="V -> R (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 464 AA; 53027 MW; 83BBAD593BEB01F5 CRC64; MGVVEGLLAL ALVLSACVMC NGGSSSPFIR KVEKTVDMPL DSDVFAVPPG YNAPQQVHIT QGDLVGKAVI VSWVTVDEPG SSEVHYWSEN SDKKKIAEGK LVTYRFFNYS SGFIHHTTIR NLEYKTKYYY EVGLGNTTRQ FWFVTPPEIG PDVPYTFGLI GDLGQSFDSN KTLSHYELNP RKGQTVLFVG DLSYADNYPN HDNIRWDSWG RFTERSVAYQ PWIWTAGNHE NHFAPEIGET VPFKPYTHRY HVPYKASQST SPFWYSIKRA SAHIIVLASY SAYGKYTPQY KWLEKELPKV NRTETPWLIV LMHSPWYNSY NYHYMEGETM RVMYEPWFVQ YKVDVVFAGH VHAYERSERV SNVAYNIVNG LCAPVNDKSA PVYITIGDGG TLEGLATNMT EPQPKYSAFR EASFGHAIFD ITNRTHAHYS WHRNQDGVAV EADSLWSFNR YWHPVDDSTA HVSH //