ID   A0A1Y2UWY9_9PEZI        Unreviewed;       535 AA.
AC   A0A1Y2UWY9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE            EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN   ORFNames=M434DRAFT_398477 {ECO:0000313|EMBL:OTA89664.1};
OS   Hypoxylon sp. CO27-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA89664.1, ECO:0000313|Proteomes:UP000194361};
RN   [1] {ECO:0000313|EMBL:OTA89664.1, ECO:0000313|Proteomes:UP000194361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO27-5 {ECO:0000313|EMBL:OTA89664.1,
RC   ECO:0000313|Proteomes:UP000194361};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(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|ARBA:ARBA00000032};
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005375}.
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DR   EMBL; KZ112529; OTA89664.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2UWY9; -.
DR   STRING; 1001938.A0A1Y2UWY9; -.
DR   Proteomes; UP000194361; Unassembled WGS sequence.
DR   GO; GO:0016158; F:3-phytase activity; IEA:UniProtKB-EC.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567:SF110; ACID PHOSPHATASE 1, ISOFORM B; 1.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000194361}.
FT   REGION          394..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   535 AA;  59356 MW;  A9856BE51EC38708 CRC64;
     MTTLTPRPPY TDDELKKLYP ANLELQLVQV LLRHGERSPV SARFQNAGLP AFWPYCSAVR
     QLKSAVLDRH HHQFSTFEWK RRLETFGPQD DPVLAAGPAG ELDGVCEMGM LTDKGRETTF
     DLGARLRSLY VDRLRFLPPV LLNADSLYLR ATPIPRALDS VQETFTGLYP AHTRAPAFPA
     PAILTRAPGD ETLFPNDSNC RRFAALSRAF AQRAADRWNN TDDMAYLTKL LGKWMPDDSK
     RVAVDSRPRL SGIMDTINST LAHGPETRLP KEFYDDKARE IIEKIGVEEW FAGYKESREY
     RALGIGSLMG DIVGRMVGSA ERSTADGQYE VARKLESSAM RNGKGTTPIT FGLSGCHDTT
     LAAILASLGA YEDSKWPPYT SHIAIEMFRK ANPATKTANS QQQGYPTIPP SENHSTSGSS
     SEAHASSWFK PWSSWSSAKP GNPPPGIGRK RSEGLSAKER AKLENYYVRI RYNDEVVTVP
     GCKAAGKHLE GDESFCTLDA FKAIVDKFVP RNWKQECRAN LQAPAVPTKP EPAGY
//