ID A0A498JUN8_MALDO Unreviewed; 585 AA.
AC A0A498JUN8;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN ORFNames=DVH24_021401 {ECO:0000313|EMBL:RXH99599.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH99599.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH99599.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH99599.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000032,
CC ECO:0000256|RuleBase:RU361203};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC acid phosphatase family. {ECO:0000256|ARBA:ARBA00008723,
CC ECO:0000256|RuleBase:RU361203}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXH99599.1}.
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DR EMBL; RDQH01000331; RXH99599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498JUN8; -.
DR Proteomes; UP000290289; Chromosome 5.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; 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; ACID PHOSPHATASE RELATED; 1.
DR PANTHER; PTHR22953:SF86; PURPLE ACID PHOSPHATASE 10; 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; 2.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361203};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361203};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT CHAIN 23..585
FT /note="Purple acid phosphatase"
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT /id="PRO_5019610126"
FT DOMAIN 54..144
FT /note="Purple acid phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16656"
FT DOMAIN 155..353
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 379..437
FT /note="Iron/zinc purple acid phosphatase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14008"
SQ SEQUENCE 585 AA; 66840 MW; D9B01A3BB2E3D150 CRC64;
MWKMAVLVVF GLLLSLAMVC NGGITSTFVR KTESTVDMPY ESDAFQIPPG HNAPQQVHIT
QGDQEGTAMI VSWITPDEPG SSVVLFWSDK HKTKKAEGKA KQYKYHDYTS GYIHHCTIRK
LEHNTKYYYK IGIGQAERTF WFVTPPAVGP DAPYTFGLLG DLGQTFDSNK TLAHYESNPL
KGQTVLCLGD LSYADNHPNH DQVKWDTFGR FIERSAAYQP WIHTAGNHEI DYAPEIGETK
PFKPYKHRYT TPFKASGSTA PFWYSVKIAS AHIIVLSSYS SYGKYTPQYK WLEQELPKVN
RDETPWLIVL VHSPWYNSYN YHYMEGETMR VQFESWFVQH KVDVVFAGHV HAYERSERVS
NIANNLENGK CSPVKDQSAP VYITIGDGGN IEGLATNMRD PQPDYSAYRE ASFGHAIFDI
KNRTHAYYSW HRNDDGAAVK ADSMWFFNRY HHPVDDSTTT VVSAGFGLEL WNGVQWRQNK
VDMPFDSDVF KFPPSYNAPQ EVHITQGDQL GKAAIVSWVT VDEPDSSTVL YWSANSKKKK
ADDKFNTKYY YVVRIDHIER QFWFITPPEV GPDTSYTFRL IGDLG
//
