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Database: UniProt
Entry: A0A0D2EYF2_9EURO
LinkDB: A0A0D2EYF2_9EURO
Original site: A0A0D2EYF2_9EURO 
ID   A0A0D2EYF2_9EURO        Unreviewed;       551 AA.
AC   A0A0D2EYF2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE            EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN   ORFNames=PV05_00002 {ECO:0000313|EMBL:KIW59730.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW59730.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW59730.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW59730.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005375}.
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DR   EMBL; KN847317; KIW59730.1; -; Genomic_DNA.
DR   RefSeq; XP_013320314.1; XM_013464860.1.
DR   AlphaFoldDB; A0A0D2EYF2; -.
DR   STRING; 348802.A0A0D2EYF2; -.
DR   GeneID; 25321910; -.
DR   HOGENOM; CLU_020880_2_2_1; -.
DR   OrthoDB; 2721627at2759; -.
DR   Proteomes; UP000054342; 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; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR20963:SF55; PHOSPHATASE, PUTATIVE-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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054342};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..551
FT                   /note="3-phytase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002241505"
SQ   SEQUENCE   551 AA;  59333 MW;  98F0749AF056CF72 CRC64;
     MKLSILSVAL VAKAIEAAPQ KITAISNVGA STSDVYPPAG TAVNSTLFPP ESKVGFPGPT
     QTGVEAAAAQ TAPLYPYNTQ AAKSFPLVAA QPQGSNSSSN VDITRYWGNL SPWYSVSSAD
     YGLPNASPLI PDGCTINQMH LLYRHGARYP TSGAAPATFA SKLANATKGA GFQVAGELAF
     LSNWTYKLGA ELLTPFGRSQ NFLLGVEYRQ LYGELLNNFT AQKAIPVFRT ESQDRMVKTA
     ENFAAGFFGV PEYLDQVNIE ILVETLGVNN SGAPYEVCNN SNVATKGSIG TAAANKFAVN
     AFNSTLSRLN SQLSGNLTFT PTDIIAMLQL CSYETDALGY SAFCPLFTQQ DFQNYEYYFD
     LSFYYNNGPG SPVAAAQGKG YLQEFVARFT QSYPTAMSAL NQTFDNTSTY FPLTQSIYAD
     ATHEVVVLDT LTAFNLTALF NGPALNTSIN QGRNSFVASK LVPFATHFTT QILECPAMKP
     SKQIRFIVND AVVPVSGSHP GCPNDPNGLC PFDTMVSVLQ KRINEIDYNY DCFANYTATA
     GVDYNGRAPR T
//
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