ID A0A2P5DFV2_TREOI Unreviewed; 355 AA.
AC A0A2P5DFV2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN ORFNames=TorRG33x02_252730 {ECO:0000313|EMBL:PON72153.1};
OS Trema orientale (Charcoal tree) (Celtis orientalis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Trema.
OX NCBI_TaxID=63057 {ECO:0000313|EMBL:PON72153.1, ECO:0000313|Proteomes:UP000237000};
RN [1] {ECO:0000313|Proteomes:UP000237000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) 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|RuleBase:RU361203};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:PON72153.1}.
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DR EMBL; JXTC01000273; PON72153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5DFV2; -.
DR STRING; 63057.A0A2P5DFV2; -.
DR InParanoid; A0A2P5DFV2; -.
DR OrthoDB; 978516at2759; -.
DR Proteomes; UP000237000; Unassembled WGS sequence.
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:InterPro.
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; IPR040974; Fn3_PAP.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR008963; Purple_acid_Pase-like_N.
DR InterPro; IPR015914; Purple_acid_Pase_N.
DR PANTHER; PTHR45778:SF6; INACTIVE PURPLE ACID PHOSPHATASE 24-RELATED; 1.
DR PANTHER; PTHR45778; PURPLE ACID PHOSPHATASE-RELATED; 1.
DR Pfam; PF17808; fn3_PAP; 1.
DR Pfam; PF00149; Metallophos; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU361203};
KW Reference proteome {ECO:0000313|Proteomes:UP000237000};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 3..112
FT /note="Purple acid phosphatase Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF17808"
FT DOMAIN 119..223
FT /note="Purple acid phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16656"
FT DOMAIN 235..327
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
SQ SEQUENCE 355 AA; 39802 MW; 56B0BAD2F8A3A384 CRC64;
MHIGEDTQWV TVDLDYNEPA ADDWVAVFSP AKFNSSTCPP VNDPKEQTPY ICSAPIKYKY
ANESNSHYTK TGKASLRFQL INQRADFSFA LFSGGLSNPK LVAVSNFISF ANPKAPLYPR
LAQGKSWDEM TVTWTSGYNI DEAVPFVEWG MRGGNQVRSP AGTLTFGRHS MCGSPARTVG
WRDPGFIHTS FLKNLWPNTV YTYRMGHLLS NGLYVWSRIY SFKSSPYPGQ DSLQRIIVFG
DMGKAERDGS NEYSNYQPGS LNTTDQIVRD LSNVDIVFHI GDITYANGYI SQWDQFTSQV
EPIASTVPYM IASGNHERDW PNSGSFYDKT DSGGECGVLA ETMFYVPAEN RAKFW
//
