ID A0A0F4ZLQ9_9PEZI Unreviewed; 466 AA.
AC A0A0F4ZLQ9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN ORFNames=TD95_000574 {ECO:0000313|EMBL:KKA31140.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA31140.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA31140.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA31140.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKA31140.1}.
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DR EMBL; LAEV01000051; KKA31140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4ZLQ9; -.
DR OrthoDB; 2721627at2759; -.
DR Proteomes; UP000033483; 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; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR20963:SF43; PUTATIVE (AFU_ORTHOLOGUE AFUA_7G01240)-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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000033483}.
FT ACT_SITE 60
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT ACT_SITE 329
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT DISULFID 235..248
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 417..426
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 466 AA; 51382 MW; 3FEE1AD8543E171F CRC64;
MPNAPLQTAV PIAAAPPNAP SIFRLMGNLS PYTPAAGFGV HEFPLPPGAR VAQLHMLSRH
GARYPTTGSL VARFGKRLAD AKKELMARDR LAFLNEWEYR LGAEILVPKG RQELYESGVL
HAYMYGALYD PSSKIIARTT TQDRMLKSAE NFMAGFFGLE WTNNATLELI IEEVGYNNSL
AGYMNCPNAN EDSGGAKARD EWANVYLQNA TERLKSMIDG YNWTIQDTYA AQTLCPYETV
AYGYSVFCDL FTYQEWEDFS YSLDLDFSAS SGFQSPTGRA VGIGYQQEFI ARLENRTLGY
SNSQINTTLD SDQATFPLNQ SLYFDFSHDS NIISVLAAFG LRQFADNLKP TANPGAHNFS
VVDLTPFGAR LDIEIIVAPK PVAADRSGYV DAGGETHYVH FVLNQRTVPL GASFAECDAA
RVDGWCELET FLAVQKKMPE KAAYDRACHG RIAADQFGKV TDGVAI
//
