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Database: UniProt
Entry: D5GM01_TUBMM
LinkDB: D5GM01_TUBMM
Original site: D5GM01_TUBMM 
ID   D5GM01_TUBMM            Unreviewed;       456 AA.
AC   D5GM01;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE            EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN   ORFNames=GSTUM_00010340001 {ECO:0000313|EMBL:CAZ85463.1};
OS   Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ85463.1, ECO:0000313|Proteomes:UP000006911};
RN   [1] {ECO:0000313|EMBL:CAZ85463.1, ECO:0000313|Proteomes:UP000006911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28 {ECO:0000313|EMBL:CAZ85463.1,
RC   ECO:0000313|Proteomes:UP000006911};
RX   PubMed=20348908; DOI=10.1038/nature08867;
RA   Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA   Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA   Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA   Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA   Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA   Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA   Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA   Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA   Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA   Ottonello S., Wincker P.;
RT   "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT   of symbiosis.";
RL   Nature 464:1033-1038(2010).
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; FN430351; CAZ85463.1; -; Genomic_DNA.
DR   RefSeq; XP_002841272.1; XM_002841226.1.
DR   AlphaFoldDB; D5GM01; -.
DR   STRING; 656061.D5GM01; -.
DR   EnsemblFungi; CAZ85463; CAZ85463; GSTUM_00010340001.
DR   GeneID; 9182766; -.
DR   KEGG; tml:GSTUM_00010340001; -.
DR   eggNOG; KOG3720; Eukaryota.
DR   HOGENOM; CLU_030431_3_1_1; -.
DR   InParanoid; D5GM01; -.
DR   OMA; SWPPFTS; -.
DR   OrthoDB; 5486499at2759; -.
DR   Proteomes; UP000006911; 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:UP000006911}.
SQ   SEQUENCE   456 AA;  51690 MW;  BC90E219A2419C03 CRC64;
     MTTLDPRPPY SPDELAALYP SNLQLHLVHV IFRHGERTPV VSRFQNAGLA PFWPYCQAAS
     RFKAAVMEPR AGWSFLTFQR RMETFGKKGE NVVATGPGGE RGNVCLLGEL TDRGRETTLQ
     LGQRLRHLYI RQLGFLPENL GSQSEYYLRA SPITRAIESL EQVFIGLYPS TNRSPTDPPA
     TIYTRSFAEE NLYPNDSGCK RLRQLTRAFS KLAAEKWNDS PEMQHLQSRI GKWVDGKIAV
     DGHPSLFGIF DSVNSTLAHG EATKLPNEFY EPRVREIMSD INVDEWYRGF NQSSEYRRLG
     VGSLLGDVKD RMLASVKHDT NEDGRLKIGL MGCHDTTIGG LLASLGGFDE KWPPFTSSIA
     FEMFREKERN KSRGVFSKLF GAKNEEEGWY VRLRYNDKPV YVKSCRVTGR HLEGDESFCT
     LTAFKEIVER MVPQDWKGEC LSNVDKTGIP PIEEVE
//
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