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   25-MAY-2022, entry version 68.
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; 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.
CC   -!- FUNCTION: Catalyzes the hydrolysis of inorganic orthophosphate from
CC       phytate. {ECO:0000250}.
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   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   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; YLMDLCP; -.
DR   OrthoDB; 1046588at2759; -.
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; -; 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   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..466
FT                   /note="3-phytase A"
FT                   /id="PRO_0000283713"
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;  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