ID A0A2H3I9R4_9EURO Unreviewed; 617 AA.
AC A0A2H3I9R4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN ORFNames=PENO1_062130 {ECO:0000313|EMBL:PCG97663.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG97663.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG97663.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG97663.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
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 -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC acid phosphatase family. {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:PCG97663.1}.
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DR EMBL; NPFK01000180; PCG97663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3I9R4; -.
DR STRING; 290292.A0A2H3I9R4; -.
DR OrthoDB; 203742at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
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; IPR014390; Acid_Pase_Asper.
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:SF159; PURPLE ACID PHOSPHATASE; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF14008; Metallophos_C; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR PIRSF; PIRSF000900; Acid_Ptase_Asper; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361203};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361203}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT CHAIN 24..617
FT /note="Purple acid phosphatase"
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT /id="PRO_5013424832"
FT DOMAIN 85..178
FT /note="Purple acid phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16656"
FT DOMAIN 280..506
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 536..599
FT /note="Iron/zinc purple acid phosphatase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14008"
SQ SEQUENCE 617 AA; 67938 MW; E6953898AB1D0598 CRC64;
MKATTASALL AALSATTFTA VNAAPAPDVD ETYPYNGPAI PVGDWVDPTV NGNGKGFPRL
VEAPAVQPKH KNPTNNINVI SLAFMPKGIN VHYQTPFGLG EAPKIKYGTN PKKLHQEATG
YSHTYDRTPP CSAVAAVTQC SQFFHEVQLR DLMPSTKYYY QIAAANGTTE SDVLSFTTSR
PAGTPGEFSL AVLNDMGYTN AGGTFKQLQK AVDAGAVFAW HGGDLSYADD WYSGILPCAD
DWPVCYNGTS SSLPAGDYPD SYNDPLPEGE IPNQGGPQGG DMSVLYESNW DLWQQWLLNV
TTKVPYMTVV GNHEAACAEF DGPGNPLTAL LDNGELNSTA AKAELTYYSC PPSQRNFTAY
QHRFWNPGNE TGGVGNFWYS FDYGLAHFIT LDGETDFVGS PEWPFARDLK GNETHPKENE
TYITDSGPFG RVSNYSDNKA YEQYQWLKAD LEKVDRSLTP WVFVMSHRPM YSSAFSSYMT
NIKNAWQDLL LEHQVDAYLS GHIHWYERMF PLTANGTVLE SAIVNNHTYY TSPGEAMTHV
VNGMAGNIES HSTLSAKQSV QNITAFLDQT HFGLSKMTVF NETAVKWEFI RGDDGSIGDY
LWLLKKESDT TPPDDTC
//
