ID A0A395SF18_FUSSP Unreviewed; 484 AA.
AC A0A395SF18;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN ORFNames=FSPOR_3694 {ECO:0000313|EMBL:RGP71006.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP71006.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP71006.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP71006.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RGP71006.1}.
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DR EMBL; PXOF01000048; RGP71006.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395SF18; -.
DR STRING; 5514.A0A395SF18; -.
DR Proteomes; UP000266152; 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:SF23; 3-PHYTASE; 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:UP000266152};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..484
FT /note="3-phytase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017480924"
FT ACT_SITE 81
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT ACT_SITE 349
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT DISULFID 70..398
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 262..276
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 423..431
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 484 AA; 53706 MW; D6E96471C11557FD CRC64;
MKAPIVAVAV LGTCCQASHA QSGSSIDPVQ PVLLPDTAAA KNPLSHLGGN GPWHIGADIT
GISSDVPEGC QVDQAAYVSR HGSRYPDTGA HNGWLEMQRK FQESDYTATG PLEFLHNWKS
PLTNPEIQIA QLSKTGYKEL FDMGYTIRTR YPDLYREGEE FVVWANNYTR VIQTAQLFLH
GFLGTNSSLG TVVSVTGKGM PAHLGDTLAP SDMCPTFVDD STKQTDAWQS KWLPAFKKRL
SQYIEGDLDL EDGQWNDFPY ICGFESQITG RLSPFCSTFN QKELEQYEYQ QDLRYYYGVG
PATKVASKMM VPFLDALVQR FVAGPDATGT NFDGKDFKLP KILMSFLNDG QLNELAVATG
VYDNQKRLPV DRIPEDRLWR NSEISPMRGT IAFERLTCTK KGRPGQKYMR ILINDRVYPV
PSCKDGPGRS CALAKYAKIT KDRLKKNGNF AKLCNATDPA TPSKVLGASF FTDLAQPHLK
PVKP
//
