ID   PPA19_ARATH             Reviewed;         388 AA.
AC   Q9LX83;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 131.
DE   RecName: Full=Purple acid phosphatase 19;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=PAP19; OrderedLocusNames=At3g46120; ORFNames=F12M12.90;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12021284; DOI=10.1074/jbc.m204183200;
RA   Li D., Zhu H., Liu K., Liu X., Leggewie G., Udvardi M., Wang D.;
RT   "Purple acid phosphatases of Arabidopsis thaliana. Comparative analysis and
RT   differential regulation by phosphate deprivation.";
RL   J. Biol. Chem. 277:27772-27781(2002).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=16244908; DOI=10.1007/s11103-005-0183-0;
RA   Zhu H., Qian W., Lu X., Li D., Liu X., Liu K., Wang D.;
RT   "Expression patterns of purple acid phosphatase genes in Arabidopsis organs
RT   and functional analysis of AtPAP23 predominantly transcribed in flower.";
RL   Plant Mol. Biol. 59:581-594(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   -!- 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=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in flowers.
CC       {ECO:0000269|PubMed:16244908}.
CC   -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC       acid phosphatase family. {ECO:0000305}.
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DR   EMBL; AL355775; CAB90939.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78116.1; -; Genomic_DNA.
DR   PIR; T49253; T49253.
DR   RefSeq; NP_190198.1; NM_114481.1.
DR   AlphaFoldDB; Q9LX83; -.
DR   SMR; Q9LX83; -.
DR   STRING; 3702.Q9LX83; -.
DR   GlyCosmos; Q9LX83; 5 sites, No reported glycans.
DR   PaxDb; 3702-AT3G46120-1; -.
DR   EnsemblPlants; AT3G46120.1; AT3G46120.1; AT3G46120.
DR   GeneID; 823755; -.
DR   Gramene; AT3G46120.1; AT3G46120.1; AT3G46120.
DR   KEGG; ath:AT3G46120; -.
DR   Araport; AT3G46120; -.
DR   TAIR; AT3G46120; PAP19.
DR   eggNOG; KOG1378; Eukaryota.
DR   HOGENOM; CLU_013387_0_1_1; -.
DR   InParanoid; Q9LX83; -.
DR   OMA; RYWSAND; -.
DR   OrthoDB; 203742at2759; -.
DR   PhylomeDB; Q9LX83; -.
DR   BioCyc; ARA:AT3G46120-MONOMER; -.
DR   PRO; PR:Q9LX83; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LX83; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003993; F:acid phosphatase activity; ISS:TAIR.
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   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:SF120; PURPLE ACID PHOSPHATASE 11-RELATED; 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.
DR   Genevisible; Q9LX83; AT.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Iron; Metal-binding; Reference proteome; Secreted;
KW   Signal; Zinc.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..388
FT                   /note="Purple acid phosphatase 19"
FT                   /id="PRO_0000372822"
FT   ACT_SITE        248
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         275..277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         275
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        348
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   388 AA;  44053 MW;  8F253A1F649CCDB0 CRC64;
     MGLNHLTLVC SAIALLSIFV VSQAGVTSTH VRVSEPSEEM PLETFPPPAC YNAPEQVHIT
     QGDHAGRGMI ISWVTPLNED GSNVVTYWIA NSDGSDNKSA LATTSSYRYF NYTSGYLYHA
     TIKGLETLYN YMSNPKGQAV LFAGDLSYAD DHPNHDQRKW DSYGRFVEPS AAYQPWIWAA
     GNHEIDYAES IPHKVHLHFG TKSNELQLTS SYSPLTQLMD ELKKVNRSET PWLIVLVHAP
     WYNSNNYHYM EGESMRVTFE PWFVENKVDI VFAGHVHAYE RSERISNIQY NITDGMSTPV
     KDQNAPVYIT IGDGGNIEGI ANNFIDPQPS YSAFREASFG HAILEIKNRT HAHYTWHRNK
     EDEFIPEAVI ADSIWLKNRY YLREEETS
//