PHYA2_ASPTE
ID PHYA2_ASPTE Reviewed; 466 AA.
AC O00100;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 83.
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].
RC STRAIN=ATCC 10020 / NRRL 1960 / CBS 116.46 / IFO 6123 / DSM 826 / IMI
RC 44243;
RA Pasamontes L., Haiker M., Henriquez Huecas M., Hug D., Mitchell D.B.,
RA Broger C., van Loon A.P.;
RT "Cloning of the phytases of Aspergillus nidulans and Talaromyces
RT thermophilus and their evolutionary relation to other histidine acid
RT phosphatases.";
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 20-35, AND SUBUNIT.
RC STRAIN=ATCC 10020 / NRRL 1960 / CBS 116.46 / IFO 6123 / DSM 826 / IMI
RC 44243;
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=23.2 uM for phytate {ECO:0000269|PubMed:9925555};
CC pH dependence:
CC Optimum pH is 5.5. Active from 4 to 6.5.
CC {ECO:0000269|PubMed:9925555};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9925554}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
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DR EMBL; U60412; AAB58465.1; -; Genomic_DNA.
DR AlphaFoldDB; O00100; -.
DR SMR; O00100; -.
DR VEuPathDB; FungiDB:ATEG_05333; -.
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:0000269|PubMed:9925554"
FT CHAIN 20..466
FT /note="3-phytase A"
FT /id="PRO_0000283712"
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 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"
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; 51055 MW; F2AECEC1AF7C22C4 CRC64;
MGVFVVLLSI ATLFGSTSGT ALGPRGNHSD CTSVDRGYQC FPELSHKWGL YAPYFSLQDE
SPFPLDVPDD CHITFVQVLA RHGARSPTDS KTKAYAATIA AIQKNATALP GKYAFLKSYN
YSMGSENLNP FGRNQLQDLG AQFYRRYDTL TRHINPFVRA ADSSRVHESA EKFVEGFQNA
RQGDPHANPH QPSPRVDVVI PEGTAYNNTL EHSICTAFEA STVGDAAADN FTAVFAPAIA
KRLEADLPGV QLSADDVVNL MAMCPFETVS LTDDAHTLSP FCDLFTAAEW TQYNYLLSLD
KYYGYGGGNP LGPVQGVGWA NELIARLTRS PVHDHTCVNN TLDANPATFP LNATLYADFS
HDSNLVSIFW ALGLYNGTKP LSQTTVEDIT RTDGYAAAWT VPFAARAYIE MMQCRAEKQP
LVRVLVNDRV MPLHGCAVDN LGRCKRDDFV EGLSFARAGG NWAECF
