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
//