PPA15_ARATH
ID PPA15_ARATH Reviewed; 532 AA.
AC Q9SFU3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Purple acid phosphatase 15;
DE EC=3.1.3.-;
DE EC=3.1.3.2;
DE AltName: Full=Phytase;
DE Flags: Precursor;
GN Name=PAP15; Synonyms=AT1; OrderedLocusNames=At3g07130; ORFNames=T1B9.21;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
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).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=18065557; DOI=10.1104/pp.107.109934;
RA Zhang W., Gruszewski H.A., Chevone B.I., Nessler C.L.;
RT "An Arabidopsis purple acid phosphatase with phytase activity increases
RT foliar ascorbate.";
RL Plant Physiol. 146:431-440(2008).
CC -!- FUNCTION: Acid phosphatase activity with p-nitrophenyl phosphate
CC (pNPP), D-myoinositol 1-phosphate (Ins(1)P1), phytic acid and Myo-
CC inositol hexakisphosphate. Low or no activity with Glc-6-P and ATP.
CC Confers shoot growth stimulation, enhanced salt and osmotic stress
CC tolerance, and ABA insensitivity. May modulate ascorbic acid (AsA)
CC levels by controlling the input of myoinositol into this branch of AsA
CC biosynthesis. {ECO:0000269|PubMed:18065557}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol
CC 1,2,3,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:20960,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58130,
CC ChEBI:CHEBI:58747;
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.5. {ECO:0000269|PubMed:18065557};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, cotyledons, leaves,
CC flowers and siliques. {ECO:0000269|PubMed:16244908,
CC ECO:0000269|PubMed:18065557}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC acid phosphatase family. {ECO:0000305}.
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DR EMBL; AF448726; AAN74650.1; -; mRNA.
DR EMBL; AC012395; AAF20233.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74502.1; -; Genomic_DNA.
DR RefSeq; NP_187369.1; NM_111593.3.
DR AlphaFoldDB; Q9SFU3; -.
DR SMR; Q9SFU3; -.
DR STRING; 3702.AT3G07130.1; -.
DR PaxDb; Q9SFU3; -.
DR PRIDE; Q9SFU3; -.
DR ProteomicsDB; 249015; -.
DR EnsemblPlants; AT3G07130.1; AT3G07130.1; AT3G07130.
DR GeneID; 819899; -.
DR Gramene; AT3G07130.1; AT3G07130.1; AT3G07130.
DR KEGG; ath:AT3G07130; -.
DR Araport; AT3G07130; -.
DR TAIR; locus:2098500; AT3G07130.
DR eggNOG; KOG1378; Eukaryota.
DR HOGENOM; CLU_013387_1_0_1; -.
DR InParanoid; Q9SFU3; -.
DR OMA; WGRFMQN; -.
DR PhylomeDB; Q9SFU3; -.
DR BRENDA; 3.1.3.2; 399.
DR PRO; PR:Q9SFU3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SFU3; baseline and differential.
DR Genevisible; Q9SFU3; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008707; F:4-phytase activity; IEA:RHEA.
DR GO; GO:0003993; F:acid phosphatase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009846; P:pollen germination; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR CDD; cd00839; MPP_PAPs; 1.
DR Gene3D; 3.60.21.10; -; 2.
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 Glycoprotein; Hydrolase; Iron; Metal-binding; Reference proteome; Secreted;
KW Signal; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..532
FT /note="Purple acid phosphatase 15"
FT /id="PRO_0000372819"
FT ACT_SITE 369
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 396..398
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
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 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 532 AA; 60435 MW; 658F6C88779444CD CRC64;
MTFLLLLLFC FLSPAISSAH SIPSTLDGPF VPVTVPLDTS LRGQAIDLPD TDPRVRRRVI
GFEPEQISLS LSSDHDSIWV SWITGEFQIG KKVKPLDPTS INSVVQFGTL RHSLSHEAKG
HSLVYSQLYP FDGLLNYTSG IIHHVRITGL KPSTIYYYRC GDPSRRAMSK IHHFRTMPVS
SPSSYPGRIA VVGDLGLTYN TTDTISHLIH NSPDLILLIG DVSYANLYLT NGTSSDCYSC
SFPETPIHET YQPRWDYWGR FMENLTSKVP LMVIEGNHEI ELQAENKTFE AYSSRFAFPF
NESGSSSTLY YSFNAGGIHF VMLGAYIAYD KSAEQYEWLK KDLAKVDRSV TPWLVASWHP
PWYSSYTAHY REAECMKEAM EELLYSYGTD IVFNGHVHAY ERSNRVYNYE LDPCGPVYIV
IGDGGNREKM AIEHADDPGK CPEPLTTPDP VMGGFCAWNF TPSDKFCWDR QPDYSALRES
SFGHGILEMK NETWALWTWY RNQDSSSEVG DQIYIVRQPD RCPLHHRLVN HC
