PPAF2_IPOBA
ID PPAF2_IPOBA Reviewed; 465 AA.
AC Q9SDZ9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Purple acid phosphatase 2;
DE EC=3.1.3.2;
DE AltName: Full=Manganese(II) purple acid phosphatase 2;
DE Flags: Precursor;
GN Name=PAP2;
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).
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 Kinetic parameters:
CC KM=95 uM for p-NPP (at pH 4.9 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:10510276};
CC KM=120 uM for ATP (at pH 4.9 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:10510276};
CC KM=180 uM for ADP (at pH 4.9 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:10510276};
CC KM=360 uM for AMP (at pH 4.9 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:10510276};
CC KM=75 uM for pyrophosphate (at pH 4.9 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:10510276};
CC KM=490 uM for beta-glycerophosphate (at pH 4.9 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:10510276};
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; AF200826; AAF19822.1; -; mRNA.
DR PIR; T51095; T51095.
DR AlphaFoldDB; Q9SDZ9; -.
DR SMR; Q9SDZ9; -.
DR BioCyc; MetaCyc:MON-15154; -.
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 Disulfide bond; Glycoprotein; Hydrolase; Iron; Metal-binding; Secreted;
KW Signal; Zinc.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..465
FT /note="Purple acid phosphatase 2"
FT /id="PRO_5000057352"
FT ACT_SITE 325
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 352..354
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 374
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 465 AA; 53401 MW; 49C0DCBA1CD8DF72 CRC64;
MGASRTGCYL LAVVLAAVMN AAIAGITSSF IRKVEKTVDM PLDSDVFRVP PGYNAPQQVH
ITQGDHVGKA MIVSWVTVDE PGSSKVVYWS ENSQHKKVAR GNIRTYTYFN YTSGYIHHCT
IRNLEYNTKY YYEVGIGNTT RSFWFTTPPE VGPDVPYTFG LIGDLGQSFD SNRTLTHYER
NPIKGQAVLF VGDLSYADNY PNHDNVRWDT WGRFVERSTA YQPWIWTAGN HEIDFAPEIG
ETKPFKPFTK RYHVPYKASG STETFWYPIK RASAYIIVLS SYSAYGKYTP QYKWLEEELP
KVNRTETPWL IVLMHSPWYN SYNYHYMEGE TMRVMYEPWF VQHKVDLVFA GHVHAYERSE
RVSNVAYDIV NGKCTPVRDQ SAPVYITIGD GGNLEGLATN MTDPQPEYSA FREASFGHAT
LDIKNRTHAY YSWHRNQDGY AVEADSMWVS NRFWHPVDDS TTTKL
