ID V9NC93_MANES Unreviewed; 611 AA.
AC V9NC93;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN Name=PAP1 {ECO:0000313|EMBL:AGL44409.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:AGL44409.1};
RN [1] {ECO:0000313|EMBL:AGL44409.1}
RP NUCLEOTIDE SEQUENCE.
RA Wang H., Zhang P.;
RT "Identification of cassava purple acid phosphatases related to phosphate
RT starvation signalling.";
RL Submitted (JUL-2012) 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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; JX402079; AGL44409.1; -; mRNA.
DR AlphaFoldDB; V9NC93; -.
DR EnsemblPlants; OAY50128; OAY50128; MANES_05G110500.
DR Gramene; OAY50128; OAY50128; MANES_05G110500.
DR OMA; FKDYDHG; -.
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:SF16; INACTIVE PURPLE ACID PHOSPHATASE 1-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 2: Evidence at transcript level;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU361203};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
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..611
FT /note="Purple acid phosphatase"
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT /id="PRO_5005149379"
FT DOMAIN 46..164
FT /note="Purple acid phosphatase Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF17808"
FT DOMAIN 170..275
FT /note="Purple acid phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16656"
FT DOMAIN 287..502
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 527..586
FT /note="Iron/zinc purple acid phosphatase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14008"
SQ SEQUENCE 611 AA; 68544 MW; 2A738C319C28C12E CRC64;
MGALKLIFSA ILLLLALQQT TSHGDNPLSK IAIHKSTFSL NDLAYVEASP SVLGLTEQNS
GWVTLEYSNP VPSVNDWIGV FSPANFSASS CPSENPRVYP PLLCSAPIKY QYANYSSPEY
KDSGKGSMKL QLINQRSDFS FALFTGGFLN PKLVAVSNTV AFSNPNAPVY PRLAQGRTWN
EMTVTWTSGY GINEAEPFIE WAPKGGDPIH SPAGTLTFDR SSMCGAPART VGWRDPGYIH
TSFLKDLWPN KVYTYKLGHK LFNGTCIWSR EYQFKASPYP GQNSVQRVVI FGDMGKGEVD
GSCEYNDFQP GSLNTTKQLI QELNNIDIVF HIGDICYANG YLSQWDQFTA QIEPIASTVP
YMIASGNHER DWPGTGSFYG NMDSGGECGV LAETMFYVPA ENRAKFWYST DYGMFRFCIA
DTEHDWREGT EQYKFIENCL ASVDRQKQPW LIFLAHRVLG YSSCITYAIE GSFQEPMGRE
SLQKLWQKYK VDIAMYGHVH NYERTCPIYQ NICTSKEKHY YKGSLNGTIH VVAGGAGASL
SPYTTLQTSW SLYKDYDHGF VKLTAFDHSN LLFEYKKSRD GKVYDSFRIS RDYRDILACT
VDSCPSKTLA S
//
