ID A0A0H1BFJ2_9EURO Unreviewed; 528 AA.
AC A0A0H1BFJ2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Phytase A {ECO:0000256|ARBA:ARBA00044106};
DE EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
DE AltName: Full=Histidine acid phosphatase phyA {ECO:0000256|ARBA:ARBA00044262};
DE AltName: Full=Myo-inositol hexakisphosphate phosphohydrolase A {ECO:0000256|ARBA:ARBA00042300};
DE AltName: Full=Myo-inositol-hexaphosphate 3-phosphohydrolase A {ECO:0000256|ARBA:ARBA00041857};
GN ORFNames=EMPG_14348 {ECO:0000313|EMBL:KLJ10269.1};
OS Blastomyces silverae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060906 {ECO:0000313|EMBL:KLJ10269.1, ECO:0000313|Proteomes:UP000053573};
RN [1] {ECO:0000313|Proteomes:UP000053573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 139 {ECO:0000313|Proteomes:UP000053573};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-
CC inositol 1,2,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77115,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798,
CC ChEBI:CHEBI:195535; Evidence={ECO:0000256|ARBA:ARBA00043748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77116;
CC Evidence={ECO:0000256|ARBA:ARBA00043748};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-
CC inositol 1,2,6-trisphosphate + phosphate; Xref=Rhea:RHEA:77119,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195535,
CC ChEBI:CHEBI:195537; Evidence={ECO:0000256|ARBA:ARBA00043670};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77120;
CC Evidence={ECO:0000256|ARBA:ARBA00043670};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,2,6-trisphosphate + H2O = 1D-myo-inositol
CC 1,2-bisphosphate + phosphate; Xref=Rhea:RHEA:77131,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195537,
CC ChEBI:CHEBI:195539; Evidence={ECO:0000256|ARBA:ARBA00043721};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77132;
CC Evidence={ECO:0000256|ARBA:ARBA00043721};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,2-bisphosphate + H2O = 1D-myo-inositol 2-
CC phosphate + phosphate; Xref=Rhea:RHEA:77135, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:195539;
CC Evidence={ECO:0000256|ARBA:ARBA00043675};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77136;
CC Evidence={ECO:0000256|ARBA:ARBA00043675};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol
CC 1,2,4,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:16989,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798,
CC ChEBI:CHEBI:58130; EC=3.1.3.8;
CC Evidence={ECO:0000256|ARBA:ARBA00043788};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16990;
CC Evidence={ECO:0000256|ARBA:ARBA00043788};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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:KLJ10269.1}.
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DR EMBL; LDEV01002111; KLJ10269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H1BFJ2; -.
DR STRING; 2060906.A0A0H1BFJ2; -.
DR OrthoDB; 2721627at2759; -.
DR Proteomes; UP000053573; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 InterPro; IPR016274; Histidine_acid_Pase_euk.
DR PANTHER; PTHR20963:SF24; 3-PHYTASE B; 1.
DR PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000894-2};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053573};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 58..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 13..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT ACT_SITE 420
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT DISULFID 89..98
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 129..472
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 273..526
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 322..340
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 497..505
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 528 AA; 58521 MW; 6DA7E0592FC3D36B CRC64;
MVEINDQTAL LACPDADGRG DQDVGSRTST SLDISDSNRR RWPHFDRKHA ASSLRERCVT
VSVVICLMLI CTAFIYAFVA RNSGRDLVCT TVQNGYQCHQ KYSQSWGQYS PFFSLETLSD
ISPQVPIGCT VTFVQVLSRH GARYPTEKKS AIYSQLIKHI QDRTETYHDD FAFLETFTYP
LQSDDLTSFG VSQMIDSGTK FYRRYRHLTK ESKIFVRASG SPRVIVSAEK FIDGFHQEKL
SDPSATDKSG KPSIGVIVSE EPGSNNTLDH SNCNLFEEAK PGLVAQAEFT KAFAAPILKR
VNSHLIGANL DITDIPYLMD ICSFHTVAIT PDASTISPIC TLFTDEEWTQ YDYYNTLGKY
YGHSIGNPLG ASQGVGFVNE LIARLTNTPV IDSTTVNHTL DSNPQTFPLG LPLYADFSHD
NTMVSIFTAL GLFNGTEPLS NTTVRSPVES KGFSAAWMVP FGARAYIEKM ECDSTPVARE
PLVRVLVNDR VVPLHGCKVD TLGRCRLEDF VEGLSYARGG GDWGKCFI
//
