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
//