ID A0A074YSI3_AURSE Unreviewed; 471 AA.
AC A0A074YSI3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN ORFNames=AUEXF2481DRAFT_534 {ECO:0000313|EMBL:KER00621.1};
OS Aureobasidium subglaciale (strain EXF-2481) (Aureobasidium pullulans var.
OS subglaciale).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043005 {ECO:0000313|EMBL:KER00621.1, ECO:0000313|Proteomes:UP000030641};
RN [1] {ECO:0000313|EMBL:KER00621.1, ECO:0000313|Proteomes:UP000030641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2481 {ECO:0000313|EMBL:KER00621.1,
RC ECO:0000313|Proteomes:UP000030641};
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 -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; KL584749; KER00621.1; -; Genomic_DNA.
DR RefSeq; XP_013349034.1; XM_013493580.1.
DR AlphaFoldDB; A0A074YSI3; -.
DR STRING; 1043005.A0A074YSI3; -.
DR GeneID; 25368866; -.
DR HOGENOM; CLU_020880_3_1_1; -.
DR InParanoid; A0A074YSI3; -.
DR OMA; RGRSDWC; -.
DR OrthoDB; 2404758at2759; -.
DR Proteomes; UP000030641; 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:SF18; ACID PHOSPHATASE PHO11-RELATED; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000030641}.
FT ACT_SITE 67
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT ACT_SITE 335
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT DISULFID 56..384
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 261..274
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 425..433
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 471 AA; 52627 MW; 20EE697122C415E4 CRC64;
MSNWTSPITS IANVTQFTNV TAQGNWNLLH HLGGHGPWIP KVDGVVEGGF GPPEGCRVEQ
VHMMARHHER YPTIGTHSRM VSLHNHLRTL DFDLEGDLAF FKNWTYFMPN TQDTGQLIPT
GPYAGTLGAF KAGVDLRTRY PDLRTTAITH NQTNFWAAGS HRVIETAKFF ASGFWGLNWE
PELANLHVIP ESSKRGADTL TTGSTCKAAR KPENHHGVPD GPHASEEWMK LFMPAIIQRL
SQQNPGLKLN FHDIRAMESF CGFDLMVRGS SPWCNVFTHD EWRDLEYARD LSQYYRHGPG
NKYSAARGFP FLNATTNLLS AGTSNGSLFL SFAHDNNVLD LLSALDLFPI SGELPTDHAP
EDRSWKTSSL IPMGSRVVFE RMVCPQVFCH SNAPLYPNHI YCDPPHDEPY VRIVINDGVV
ATPDCDDGPG KSCPLASFER RVMLKGWEVG DFGRVCELEE GAPNKITFLH Q
//
