PHYA1_ASPTE
ID PHYA1_ASPTE Reviewed; 466 AA.
AC O00085;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=3-phytase A;
DE EC=3.1.3.8;
DE AltName: Full=3 phytase A;
DE AltName: Full=Myo-inositol hexakisphosphate phosphohydrolase A;
DE AltName: Full=Myo-inositol-hexaphosphate 3-phosphohydrolase A;
DE Flags: Precursor;
GN Name=phyA;
OS Aspergillus terreus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=33178;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=9A1;
RX PubMed=9025298; DOI=10.1099/00221287-143-1-245;
RA Mitchell D.B., Vogel K., Weimann B.J., Pasamontes L., van Loon A.P.G.M.;
RT "The phytase subfamily of histidine acid phosphatases: isolation of genes
RT for two novel phytases from the fungi Aspergillus terreus and
RT Myceliophthora thermophila.";
RL Microbiology 143:245-252(1997).
RN [2]
RP PROTEIN SEQUENCE OF 29-38 AND 192-200, AND SUBUNIT.
RC STRAIN=9A1;
RX PubMed=9925554; DOI=10.1128/aem.65.2.359-366.1999;
RA Wyss M., Pasamontes L., Friedlein A., Remy R., Tessier M., Kronenberger A.,
RA Middendorf A., Lehmann M., Schnoebelen L., Roethlisberger U., Kusznir E.,
RA Wahl G., Mueller F., Lahm H.-W., Vogel K., van Loon A.P.G.M.;
RT "Biophysical characterization of fungal phytases (myo-inositol
RT hexakisphosphate phosphohydrolases): molecular size, glycosylation pattern,
RT and engineering of proteolytic resistance.";
RL Appl. Environ. Microbiol. 65:359-366(1999).
RN [3]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 hydrolysis of inorganic orthophosphate from
CC phytate. Releases 5 of the 6 phosphate groups to yield the end product
CC myo-inositol 2-monophosphate. Specific for phytate.
CC {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;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.6 uM for phytate {ECO:0000269|PubMed:9925555};
CC pH dependence:
CC Optimum pH is 5.5. Active from 2.5 to 7.5 with phytic acid as
CC substrate. The optimum pH is shifted to more acidic values with 4-
CC nitrophenyl phosphate as substrate. {ECO:0000269|PubMed:9925555};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9925554}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
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DR EMBL; U59805; AAB52507.1; -; Genomic_DNA.
DR AlphaFoldDB; O00085; -.
DR SMR; O00085; -.
DR VEuPathDB; FungiDB:ATEG_05333; -.
DR BRENDA; 3.1.3.26; 536.
DR BRENDA; 3.1.3.8; 536.
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; -; 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 Pfam; PF00328; His_Phos_2; 1.
DR PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..466
FT /note="3-phytase A"
FT /id="PRO_0000023972"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 362
FT /note="Proton donor"
FT /evidence="ECO:0000250"
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"
FT DISULFID 71..414
FT /evidence="ECO:0000250"
FT DISULFID 215..465
FT /evidence="ECO:0000250"
FT DISULFID 264..282
FT /evidence="ECO:0000250"
FT DISULFID 436..444
FT /evidence="ECO:0000250"
SQ SEQUENCE 466 AA; 51093 MW; 21CDCB559C96AE66 CRC64;
MGFLAIVLSV ALLFRSTSGT PLGPRGKHSD CNSVDHGYQC FPELSHKWGL YAPYFSLQDE
SPFPLDVPED CHITFVQVLA RHGARSPTHS KTKAYAATIA AIQKSATAFP GKYAFLQSYN
YSLDSEELTP FGRNQLRDLG AQFYERYNAL TRHINPFVRA TDASRVHESA EKFVEGFQTA
RQDDHHANPH QPSPRVDVAI PEGSAYNNTL EHSLCTAFES STVGDDAVAN FTAVFAPAIA
QRLEADLPGV QLSTDDVVNL MAMCPFETVS LTDDAHTLSP FCDLFTATEW TQYNYLLSLD
KYYGYGGGNP LGPVQGVGWA NELMARLTRA PVHDHTCVNN TLDASPATFP LNATLYADFS
HDSNLVSIFW ALGLYNGTAP LSQTSVESVS QTDGYAAAWT VPFAARAYVE MMQCRAEKEP
LVRVLVNDRV MPLHGCPTDK LGRCKRDAFV AGLSFAQAGG NWADCF
