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Database: UniProt
Entry: Q5XNQ9_ASPFM
LinkDB: Q5XNQ9_ASPFM
Original site: Q5XNQ9_ASPFM 
ID   Q5XNQ9_ASPFM            Unreviewed;       465 AA.
AC   Q5XNQ9;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE            EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
DE   Flags: Fragment;
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:AAU93517.1};
RN   [1] {ECO:0000313|EMBL:AAU93517.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17534560; DOI=10.1007/s00284-006-0613-5;
RA   Wang Y., Gao X., Su Q., Wu W., An L.;
RT   "Cloning, expression, and enzyme characterization of an acid heat-stable
RT   phytase from Aspergillus fumigatus WY-2.";
RL   Curr. Microbiol. 55:65-70(2007).
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:ARBA00001612};
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005375}.
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DR   EMBL; AY745738; AAU93517.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5XNQ9; -.
DR   SMR; Q5XNQ9; -.
DR   BRENDA; 3.1.3.8; 508.
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|PIRSR:PIRSR000894-2};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..465
FT                   /note="3-phytase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004264450"
FT   ACT_SITE        81
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT   ACT_SITE        360
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT   DISULFID        30..39
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        70..412
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        213..463
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        262..280
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        434..442
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   NON_TER         465
FT                   /evidence="ECO:0000313|EMBL:AAU93517.1"
SQ   SEQUENCE   465 AA;  50788 MW;  1B61FBCD226BDA66 CRC64;
     MVTLTFLLSV AYLLSGRVSG APSSAGSKSC DTVELGYQCS PATSHLWGQY SPFFSLDDEL
     SVSSELPKDC RVTFVQMLSR HGARYPTSSK SKKYKQLVTA LQRNATSFKG KFAFLKTYNY
     TLGADDLTPF GEQQMVNSGI KFYQKYKALA RSVVPFIRSS GSDRVIASGE KFIEGFQQAK
     LADSGATNRA APVISVIIPE SETFNNTLDH SVCTNFEASE LGDEVAANFT ALFAPAIRAR
     AEKHLPGVKL TDDDVVSLMD MCSFDTVART SDASQLSPFC ALFTHNEWKK YDYLQSLGKY
     YGYGAGNALG PAQGIGFTNE LIARLTRSPV QDHTSTNSTL DSNPATFPLN ATIYVDFSHD
     NGMIPIFFAM GLYNGTEPLS LTSVESTKDS DGYSASWAVP FAARAYFETM QCKSEKEPLV
     RALINDRVVP LHGCAVDKLG RCKLNDFVEG LSWARSGGNW GECFS
//
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