ID A0A2C5Y5U7_9HYPO Unreviewed; 457 AA.
AC A0A2C5Y5U7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=CDD81_7311 {ECO:0000313|EMBL:PHH62251.1};
OS Ophiocordyceps australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1399860 {ECO:0000313|EMBL:PHH62251.1, ECO:0000313|Proteomes:UP000226192};
RN [1] {ECO:0000313|EMBL:PHH62251.1, ECO:0000313|Proteomes:UP000226192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map64 {ECO:0000313|EMBL:PHH62251.1,
RC ECO:0000313|Proteomes:UP000226192};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:PHH62251.1}.
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DR EMBL; NJET01000077; PHH62251.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5Y5U7; -.
DR STRING; 1399860.A0A2C5Y5U7; -.
DR OrthoDB; 2721627at2759; -.
DR Proteomes; UP000226192; 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 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000226192};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..457
FT /note="Phytase A"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013129764"
FT ACT_SITE 75
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT ACT_SITE 351
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT DISULFID 64..403
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 203..454
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 255..271
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 425..433
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 457 AA; 50171 MW; FCC4A0CA4D5FBA24 CRC64;
MCGAIIVISA IMFLLVTYGQ SLGTASHACQ DLGQCTSGTS HIWGQYSPYF SAPSSIDAAV
PKGCSLTFGL ALSRHGSRWP TAGKNEAYRS LVQRIQSSVQ RYSPGYDFIQ DYAFQLGVDG
LTPFGEQEMV DSGAAFFRRY EELAKTQQPF LRASGSDRVV MSAQNFTRGF YAAQGKSGDY
EADHILIMPE GASFNNTLDH GSCPAFENGP DSELAHVKQA AWMESWATPI RSRMNEKLPG
ANLTLQETVL MMDLCPFETV ATAQANVSDF CRLFTRDEWR GYDYFQSLGK WYGYGKGNAL
GPTQGIGYVN ELVARLTGQS VQDGTTTNST LDSSPATFPL DRQLYADFSH DNSLMTVYAA
LGLYNATQDL PVERKLSPQQ THGYSASWTV PFAARMYVEK MRCGANDEEL VRIIVNDRVV
PLQGCGSDGL GRCRLALFIE SLGFAHAGGL WDACFTW
//
