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Database: UniProt
Entry: A0A074YJ33_AURPU
LinkDB: A0A074YJ33_AURPU
Original site: A0A074YJ33_AURPU 
ID   A0A074YJ33_AURPU        Unreviewed;       461 AA.
AC   A0A074YJ33;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE            EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN   ORFNames=M438DRAFT_343344 {ECO:0000313|EMBL:KEQ86921.1};
OS   Aureobasidium pullulans EXF-150.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ86921.1, ECO:0000313|Proteomes:UP000030706};
RN   [1] {ECO:0000313|EMBL:KEQ86921.1, ECO:0000313|Proteomes:UP000030706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ86921.1,
RC   ECO:0000313|Proteomes:UP000030706};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
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; KL584977; KEQ86921.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074YJ33; -.
DR   STRING; 1043002.A0A074YJ33; -.
DR   HOGENOM; CLU_020880_0_0_1; -.
DR   OrthoDB; 2721627at2759; -.
DR   Proteomes; UP000030706; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000030706};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..461
FT                   /note="3-phytase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001704850"
FT   ACT_SITE        77
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT   ACT_SITE        356
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT   DISULFID        66..408
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        208..459
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        260..276
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        430..438
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ   SEQUENCE   461 AA;  50320 MW;  A500F22AA0BC2E4B CRC64;
     MAFAAAGLLA LGVVGSSSAL LIPKPQACDS VQSGYQCQPQ ISHFWGQYSP YFSVPSEIPA
     DVPLTCSVTF AQILSRHGAR DPTASKTAKY NSTIIKIQNN VANFTGKYAF LDDYEYTLGA
     DQLTDFGRQQ MENSGIKYYQ RYANLARKSV PFVRSSSEDR VVESAERWID GFNQTKAGDW
     WANKNYPSIN VVISEAAGSN NTLNHDLCNS FENGPDSTIA DAAQKTWVSV FVPAIQKRIN
     TDLPGANLTS TEIIYLMDLC PFNTVASPNG TISPFCSLFT ESEWHDYGYY ESLNKYYGYG
     AGNPLGPTQG IGFTNELIAR LTKKAVQDHT STNSTLDSNP VTFPLDRALY ADFSHDNDMT
     AIFFAMGLYN STAPLSNTTL QTAQQSNGYS AAYTVPFAAR AYIEKLQCLG HKEEMVRVIV
     NDRVIPLQGC GADWLGRCGL GAFVDSMAFA RSGGGWASCA V
//
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