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Database: UniProt
Entry: A0A074VSB4_9PEZI
LinkDB: A0A074VSB4_9PEZI
Original site: A0A074VSB4_9PEZI 
ID   A0A074VSB4_9PEZI        Unreviewed;       430 AA.
AC   A0A074VSB4;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE            EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN   ORFNames=M437DRAFT_46933 {ECO:0000313|EMBL:KEQ63625.1};
OS   Aureobasidium melanogenum CBS 110374.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ63625.1, ECO:0000313|Proteomes:UP000030672};
RN   [1] {ECO:0000313|EMBL:KEQ63625.1, ECO:0000313|Proteomes:UP000030672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ63625.1,
RC   ECO:0000313|Proteomes:UP000030672};
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; KL584831; KEQ63625.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074VSB4; -.
DR   STRING; 1043003.A0A074VSB4; -.
DR   HOGENOM; CLU_020880_3_2_1; -.
DR   OrthoDB; 2404758at2759; -.
DR   Proteomes; UP000030672; 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:SF56; ACID PHOSPHATASE-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; PS00616; HIS_ACID_PHOSPHAT_1; 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:UP000030672};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..430
FT                   /note="3-phytase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001700897"
FT   ACT_SITE        62
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT   ACT_SITE        321
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT   DISULFID        51..370
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        244..259
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT   DISULFID        393..401
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ   SEQUENCE   430 AA;  47058 MW;  B364643AF0B95B32 CRC64;
     MLSLSSLAQL TLVPAAAAQA FNLYEHLGNL SPYFTPPNTP PSLLSGIPES CSVDRAFLVH
     RHGSRQPISS ELPTIQNLSY YINNNTALFK NPQGQLPSEF SFLKSGWSSG FTLNNLSAPG
     RQQLFDHGVA FRLDYPSLYT DTVLAGDQDR VVESAQWFMD GYYGRYVEDV AVLNKIAEDN
     LTISWITSTD TCKTWEYSSG NDLVTDWGKV YLPSIATRMN KALSSAYPGV NFTAQHAHGA
     LWACAYGTAV YGIGRSPWCA VFKPQEILGF EYELDLLMRG AFGYGLPNDQ GPVLGSLLVS
     NVTTFLQSST GQNLSLNFAH DTTIDLGLTA LGLAYDQQYP ATGPPNPSRN WRTSTQVPFA
     AQMLFKRLSC SNNETRIQLE LNGANFDLSP VGCTSDYYGT CKLADFVATK HVQTAMNITD
     GDATWNAACL
//
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