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Database: UniProt
Entry: A0A2P5BT78_PARAD
LinkDB: A0A2P5BT78_PARAD
Original site: A0A2P5BT78_PARAD 
ID   A0A2P5BT78_PARAD        Unreviewed;       488 AA.
AC   A0A2P5BT78;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE            EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN   ORFNames=PanWU01x14_212520 {ECO:0000313|EMBL:PON52009.1};
OS   Parasponia andersonii (Sponia andersonii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX   NCBI_TaxID=3476 {ECO:0000313|EMBL:PON52009.1, ECO:0000313|Proteomes:UP000237105};
RN   [1] {ECO:0000313|Proteomes:UP000237105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
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|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:PON52009.1}.
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DR   EMBL; JXTB01000226; PON52009.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5BT78; -.
DR   STRING; 3476.A0A2P5BT78; -.
DR   OrthoDB; 203742at2759; -.
DR   Proteomes; UP000237105; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006950; P:response to stress; IEA:UniProt.
DR   CDD; cd00839; MPP_PAPs; 1.
DR   Gene3D; 3.60.21.10; -; 2.
DR   Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR003961; FN3_dom.
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:SF35; FE(3+)-ZN(2+) PURPLE ACID PHOSPHATASE 12; 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   PROSITE; PS50853; FN3; 1.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237105};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        379..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          16..122
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          459..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   488 AA;  56478 MW;  A8883FB1C619F3B4 CRC64;
     MPICSDVFRV PPGYNAPQQV HITQGDHVGK GVIVSWVTPD EPGSSRMLYW SKNSQLKNTA
     EGIVLTYKYV NYTSGDIHHC TIDNLELNTE LWFSTPLFDT KYFYEVGIGN TTRKFWFRTP
     PNVGPDVPST FGVIGDLGQT QDSNRTLAHY ELNTLKGQTV LFVVDLSYAN DYSFHDNTRW
     DTWERFLERN AAYQPWIWTA GNHELDFAPE LGESEPFKPY RSRFHVRYKA SISSSPLWYS
     IKRASAHIIV LSSYSAFGKS TPQYKWLRKE LPKVNREETL WLVLVHCPLY SSYVDHYTEG
     ESMRVVYESW FVEYKVDVVF SGHVHAYERS ERISNIAYNI VNGICTPKSD QSAPVYVTIG
     DGGNLKRTGD RACLLNIDYW SVLLADVFFF FIFYFFLFWW SCSMIEPQPS YSAYREASFG
     HGIFDIKKRS HAFFSWHRNQ DGYDVEADCI WLHNRYWNSS SPGEASRSRN KCSISEEEVS
     QSQISSYS
//
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