PPAF_SOYBN
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 03-AUG-2022, entry version 93.
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}.
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DR EMBL; AF200824; AAF19820.1; -; mRNA.
DR PIR; B59200; B59200.
DR AlphaFoldDB; Q09131; -.
DR SMR; Q09131; -.
DR STRING; 3847.GLYMA09G36360.1; -.
DR PRIDE; Q09131; -.
DR eggNOG; KOG1378; Eukaryota.
DR InParanoid; Q09131; -.
DR BioCyc; MetaCyc:MON-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 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 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
