ID PHYA_ASPTN Reviewed; 466 AA.
AC Q0CLV1;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Phytase A {ECO:0000303|PubMed:9925555};
DE EC=3.1.3.- {ECO:0000269|PubMed:9925555};
DE EC=3.1.3.8 {ECO:0000269|PubMed:9925555};
DE AltName: Full=Histidine acid phosphatase phyA {ECO:0000303|PubMed:9925555};
DE Short=HAP {ECO:0000303|PubMed:9925555};
DE AltName: Full=Myo-inositol hexakisphosphate phosphohydrolase A {ECO:0000303|PubMed:9925555};
DE AltName: Full=Myo-inositol-hexaphosphate 3-phosphohydrolase A {ECO:0000303|PubMed:9925555};
DE Flags: Precursor;
GN Name=phyA {ECO:0000303|PubMed:9925555}; ORFNames=ATEG_05333;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9925555; DOI=10.1128/aem.65.2.367-373.1999;
RA Wyss M., Brugger R., Kronenberger A., Remy R., Fimbel R., Oesterhelt G.,
RA Lehmann M., van Loon A.P.G.M.;
RT "Biochemical characterization of fungal phytases (myo-inositol
RT hexakisphosphate phosphohydrolases): catalytic properties.";
RL Appl. Environ. Microbiol. 65:367-373(1999).
CC -!- FUNCTION: Catalyzes the phosphate monoester hydrolysis of phytic acid
CC (myo-inositol hexakisphosphate), which results in the stepwise
CC formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and
CC monophosphates, as well as the liberation of inorganic phosphate
CC (PubMed:9925555). Myo-inositol 2-monophosphate is the end product
CC (PubMed:9925555). Has a broad substrate specificity and is also able to
CC dephosphorylate other classic acid phosphatase substrates such as p-
CC nitrophenyl phosphate, phenyl phosphate, fructose 1,6-bisphosphate,
CC glucose 6-phosphate, 3-phosphoglycerate, as well as ADP and ATP
CC (PubMed:9925555). {ECO:0000269|PubMed:9925555}.
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; Evidence={ECO:0000269|PubMed:9925555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16990;
CC Evidence={ECO:0000269|PubMed:9925555};
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:0000269|PubMed:9925555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77116;
CC Evidence={ECO:0000269|PubMed:9925555};
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:0000269|PubMed:9925555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77120;
CC Evidence={ECO:0000269|PubMed:9925555};
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:0000269|PubMed:9925555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77132;
CC Evidence={ECO:0000269|PubMed:9925555};
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:0000269|PubMed:9925555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77136;
CC Evidence={ECO:0000269|PubMed:9925555};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9925555}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
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DR EMBL; CH476600; EAU34402.1; -; Genomic_DNA.
DR RefSeq; XP_001214511.1; XM_001214511.1.
DR AlphaFoldDB; Q0CLV1; -.
DR SMR; Q0CLV1; -.
DR STRING; 341663.Q0CLV1; -.
DR GlyCosmos; Q0CLV1; 8 sites, No reported glycans.
DR EnsemblFungi; EAU34402; EAU34402; ATEG_05333.
DR GeneID; 4320687; -.
DR VEuPathDB; FungiDB:ATEG_05333; -.
DR eggNOG; KOG1382; Eukaryota.
DR HOGENOM; CLU_020880_0_0_1; -.
DR OMA; CRVTFAQ; -.
DR OrthoDB; 2721627at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..466
FT /note="Phytase A"
FT /id="PRO_0000283713"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O00092"
FT BINDING 51
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT BINDING 81
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT BINDING 82
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT BINDING 85
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT BINDING 88
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT BINDING 165
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT BINDING 301
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT BINDING 361
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT BINDING 362
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..40
FT /evidence="ECO:0000250|UniProtKB:O00092"
FT DISULFID 71..414
FT /evidence="ECO:0000250|UniProtKB:O00092"
FT DISULFID 215..465
FT /evidence="ECO:0000250|UniProtKB:O00092"
FT DISULFID 264..282
FT /evidence="ECO:0000250|UniProtKB:O00092"
FT DISULFID 436..444
FT /evidence="ECO:0000250|UniProtKB:O00092"
SQ SEQUENCE 466 AA; 51088 MW; 95C75138C6F10045 CRC64;
MGVFVVLLSI ATLFGSTSGT ALGPRGNHSD CNSVDHGYQC FPELSHKWGL YAPYFSLQDE
SPFPLDVPDD CQITFVQALA RHGARSPTDS KTKAYAATIA AIQKNATTFP GKYAFLKSYN
YSMGSEDLTP FGRNQLQDMG AQFYRRYDTL TRHINPFIRA ADSSRVHESA EKFVEGFQNA
RQGDPRANPH QPSPRVDVVI PEGTAYNNTL EHSICTAFED STVGDAAADN FTAVFAPAIA
KRLEADLPGV QLSADDVINL MAMCPFETVS LTDDAHTLSP FCDLFTAAEW TQYNYLLSLD
KYYGYGGGNP LGPVQGVGWA NELIARLTHS PVHDHTCVNN TLDANPATFP LNATLYADFS
HDSNLVSIFW ALGLYNGTKA LSQTTVEDTT QTDGYAAAWT VPFAARAYIE MMQCRAEKQP
LVRVLVNDRV MPLHGCAVDN LGRCKRDDFV EGLSFARAGG NWAECF
//
