ID W1PQF6_AMBTC Unreviewed; 613 AA.
AC W1PQF6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN ORFNames=AMTR_s00013p00197230 {ECO:0000313|EMBL:ERN09951.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN09951.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
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 -!- 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}.
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DR EMBL; KI392979; ERN09951.1; -; Genomic_DNA.
DR RefSeq; XP_006848370.1; XM_006848307.2.
DR AlphaFoldDB; W1PQF6; -.
DR STRING; 13333.W1PQF6; -.
DR EnsemblPlants; ERN09951; ERN09951; AMTR_s00013p00197230.
DR GeneID; 18438117; -.
DR Gramene; ERN09951; ERN09951; AMTR_s00013p00197230.
DR KEGG; atr:18438117; -.
DR eggNOG; KOG1378; Eukaryota.
DR HOGENOM; CLU_013387_4_1_1; -.
DR OMA; LAPTHIM; -.
DR OrthoDB; 456532at2759; -.
DR Proteomes; UP000017836; 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 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; IPR040974; Fn3_PAP.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041792; MPP_PAP.
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; 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; 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.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU361203};
KW Reference proteome {ECO:0000313|Proteomes:UP000017836};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
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..613
FT /note="Purple acid phosphatase"
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT /id="PRO_5005149690"
FT DOMAIN 48..164
FT /note="Purple acid phosphatase Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF17808"
FT DOMAIN 173..277
FT /note="Purple acid phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16656"
FT DOMAIN 289..504
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 529..588
FT /note="Iron/zinc purple acid phosphatase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14008"
SQ SEQUENCE 613 AA; 69104 MW; 62397BA85290E610 CRC64;
MEWVRILMFC LIWVSFWDSM NALHQGEQPL SKIAIHNTVL ALDNAAYIKA SPDLIGAEGK
NNEWVNLSFG NPNPSGDDWV GVFSPSNFNG STCAPENNRD GPPYICTAPI KYQFANFSSP
SYTTTGNGTL SLLLINQRAD FSFALFSGGF VQPKLIAVSN PISFLYPKAP LYPRLAQGKS
WNEMTVTWTS GYSIYEAVPL VEWGLKGDSQ IRSPAGTLTF TRNSMCGSPA RTVGWRDPGY
IHTAFLKNLW PNTQYTYKLG HRLFNGSYVW SKKYSFRASP YPGQDSLQRV IIFGDMGKAE
RDGSNEYNNY QPGSLNTTDQ LIKDLDNIGI VFHIGDIVYA NGYISQWDQF TSQVEPIAST
VPYMLASGNH ERDWPGTGSF YENMDSGGEC GVPAETMFYV PAENRAKYWY ATDYGMFHFC
IADTEHDWRE GSQQYKFIEQ CLASADRQKQ PWLIFLAHRV LGYSSGTWYA KQGSFEEPMG
RESLQKLWQK YKVDMAFYGH VHNYERTCPI YQSICVNQEK SHYSGIVNGT IHVVAGGGGS
HVSEFTDLKT NWSLYRDYDY GFVKLTAFDH SSLLFEYKKS SDGKVYDSFT ISRDYKDVLA
CAIDSCQPTT LAS
//
