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Purple acid phosphatase 2 (EC 3.1.3.2) (Manganese(II) purple acid phosphatase 2)

 PPAF2_IPOBA             Reviewed;         465 AA.
Q9SDZ9;
05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
05-DEC-2018, entry version 70.
RecName: Full=Purple acid phosphatase 2;
EC=3.1.3.2;
AltName: Full=Manganese(II) purple acid phosphatase 2;
Flags: Precursor;
Name=PAP2;
Ipomoea batatas (Sweet potato) (Convolvulus batatas).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae;
Ipomoea.
NCBI_TaxID=4120;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, COFACTOR, AND
BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=cv. Golden;
PubMed=10510276; DOI=10.1006/abbi.1999.1407;
Schenk G., Ge Y., Carrington L.E., Wynne C.J., Searle I.R.,
Carroll B.J., Hamilton S., de Jersey J.;
"Binuclear metal centers in plant purple acid phosphatases: Fe-Mn in
sweet potato and Fe-Zn in soybean.";
Arch. Biochem. Biophys. 370:183-189(1999).
-!- CATALYTIC ACTIVITY:
Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
Evidence={ECO:0000269|PubMed:10510276};
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
Note=Binds 1 Fe cation per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:10510276};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:10510276};
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Evidence={ECO:0000269|PubMed:10510276};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10510276};
Note=Binds 1 Mn(2+) ion per subunit. Can also use Zn(2+), Cu(2+)
and Mg(2+) ions. {ECO:0000269|PubMed:10510276};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Absorption:
Abs(max)=560 nm {ECO:0000269|PubMed:10510276};
Kinetic parameters:
KM=95 uM for p-NPP (at pH 4.9 and 25 degrees Celsius)
{ECO:0000269|PubMed:10510276};
KM=120 uM for ATP (at pH 4.9 and 25 degrees Celsius)
{ECO:0000269|PubMed:10510276};
KM=180 uM for ADP (at pH 4.9 and 25 degrees Celsius)
{ECO:0000269|PubMed:10510276};
KM=360 uM for AMP (at pH 4.9 and 25 degrees Celsius)
{ECO:0000269|PubMed:10510276};
KM=75 uM for pyrophosphate (at pH 4.9 and 25 degrees Celsius)
{ECO:0000269|PubMed:10510276};
KM=490 uM for beta-glycerophosphate (at pH 4.9 and 25 degrees
Celsius) {ECO:0000269|PubMed:10510276};
-!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- SIMILARITY: Belongs to the metallophosphoesterase superfamily.
Purple acid phosphatase family. {ECO:0000305}.
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EMBL; AF200826; AAF19822.1; -; mRNA.
PIR; T51095; T51095.
ProteinModelPortal; Q9SDZ9; -.
SMR; Q9SDZ9; -.
BioCyc; MetaCyc:MONOMER-15154; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
Gene3D; 2.60.40.380; -; 1.
Gene3D; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
InterPro; IPR039331; PPA-like.
InterPro; IPR008963; Purple_acid_Pase-like_N.
InterPro; IPR015914; Purple_acid_Pase_N.
InterPro; IPR025733; Purple_acid_PPase_C_dom.
PANTHER; PTHR22953; PTHR22953; 1.
Pfam; PF00149; Metallophos; 1.
Pfam; PF14008; Metallophos_C; 1.
Pfam; PF16656; Pur_ac_phosph_N; 1.
SUPFAM; SSF49363; SSF49363; 1.
1: Evidence at protein level;
Disulfide bond; Glycoprotein; Hydrolase; Iron; Metal-binding;
Secreted; Signal; Zinc.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 465 Purple acid phosphatase 2.
/FTId=PRO_5000057352.
REGION 352 354 Substrate binding. {ECO:0000250}.
ACT_SITE 325 325 Proton donor. {ECO:0000250}.
METAL 164 164 Iron. {ECO:0000250}.
METAL 193 193 Iron. {ECO:0000250}.
METAL 193 193 Manganese. {ECO:0000250}.
METAL 196 196 Iron. {ECO:0000250}.
METAL 230 230 Manganese. {ECO:0000250}.
METAL 315 315 Manganese. {ECO:0000250}.
METAL 352 352 Manganese. {ECO:0000250}.
METAL 354 354 Iron. {ECO:0000250}.
BINDING 230 230 Substrate. {ECO:0000250}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 303 303 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 400 400 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 425 425 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 374 374 Interchain. {ECO:0000250}.
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


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