ID A0A0D2EK91_9EURO Unreviewed; 577 AA.
AC A0A0D2EK91;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN ORFNames=PV05_07346 {ECO:0000313|EMBL:KIW55030.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW55030.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW55030.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW55030.1,
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 -!- 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; KN847320; KIW55030.1; -; Genomic_DNA.
DR RefSeq; XP_013315614.1; XM_013460160.1.
DR AlphaFoldDB; A0A0D2EK91; -.
DR STRING; 348802.A0A0D2EK91; -.
DR GeneID; 25329254; -.
DR HOGENOM; CLU_030431_3_1_1; -.
DR OrthoDB; 5486499at2759; -.
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; 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:UP000054342}.
FT REGION 399..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 63858 MW; 3DB148D2FD8FB900 CRC64;
MTTLAPRSPY TQEELDKFYP KGLELRLVQV LLRHGERAPV SARFGNAGLP AYWPYCNAAQ
RLRSVTMTTD DISRWDSLQW RRRLETFGDD DGPLVAAGPA GEVDGICQFG ELTDKGRDTT
YELGRRLRHL YVEQLQFMPK LIANADLIYL RATPLPRALE SVQQTFWGMY PLTARTASFP
APTIVTRTPA DETLFPNDGN CRRFAQLSRA FAQRAADRWN ETDDMKYLTK LIGKWMPESS
NKTVAVDSHP RLSGIMDTIN STLAHGPETR LPREFYDSKA REIIDRIGVE EWFHGYNENR
EYRMLGIGGL MGDIVERMTS KVEGAGLSIN EIGGENGRLG KGRGGEMGIR FAMSGCHDTT
LAGVLTSLGA FNGEKWPPYT SHIAFELFRK AGADGGDGKH ADADFLTPTT PASTEPKRQK
EEEVVKPGLF ASFLGLKSPK AHPDPAEKLQ SGSVSGSDPL STPKLSRGSS GIATSIPPKD
LIARSAWSEL SEKQKGRLDG YYVRVRYNDK VMKVPACAQP GNNYQGDETL CTFEAFKRVV
DGYTPKNWKV QCGQNLDKPV DGLGSPAQMA GQIEEGF
//
