ID I2DBZ5_ASPFM Unreviewed; 467 AA.
AC I2DBZ5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, 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 Name=phy {ECO:0000313|EMBL:AFJ79737.1};
OS Aspergillus fumigatus (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=746128 {ECO:0000313|EMBL:AFJ79737.1};
RN [1] {ECO:0000313|EMBL:AFJ79737.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MI 3 {ECO:0000313|EMBL:AFJ79737.1};
RA Mishra I.G., Bhurat K.B., Tripathi N., Tantwai K., Tiwari S.;
RT "Molecular cloning and characterization of phytase gene from Aspergillus
RT fumigatus.";
RL Submitted (FEB-2012) 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}.
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DR EMBL; JQ654451; AFJ79737.1; -; Genomic_DNA.
DR AlphaFoldDB; I2DBZ5; -.
DR SMR; I2DBZ5; -.
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, ECO:0000313|EMBL:AFJ79737.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..467
FT /note="Phytase A"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003656614"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT ACT_SITE 362
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT DISULFID 31..40
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 71..414
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 215..465
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 264..282
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 436..444
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 467 AA; 50971 MW; FA3AACD98C2B7284 CRC64;
MGVSAVLLPL YLLSGVTSGL AVPASRNQST CDTVDQGYQC FSETSHLWGQ YAPFFSLANK
SAISPDVPAG CHVTFAQVLS RHGARYPTDS KGKKYSALIE EIQQNATTFE GKYAFLKTYN
YSLGADDLTP FGEQELVNSG VKFYQRYESL TRNIVPFIRS SGSSRVIASG NKFIEGFQST
KLKDPRAQPG QSSPKIDVVI SEASTSNNTL DPGTCTVFED SELADDIEAN FTATFVPSIR
QRLENDLSGV SLTDTEVTYL MDMCSFDTIS TSTVDTKLSP FCDLFTHEGW INYDYLQSLN
KYYGHGAGNP LGPTQGVGYA NELIARLTHS PVHDDTSSNH TLDSNPATFP LNSTLYADFS
HDNGIISILF ALGLYNGTKP LSSTTAENIT QTDGFSSAWT VPFASRMYVE MMQCQSEQEP
LVRVLVNDRV VPLHGCPVDA LGRCTRDSFV KGLSFARSGG DWAECFA
//
