ID A0A084Q8G4_STAC4 Unreviewed; 518 AA.
AC A0A084Q8G4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN ORFNames=S40285_08077 {ECO:0000313|EMBL:KFA60249.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA60249.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA60249.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA60249.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; KL660941; KFA60249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084Q8G4; -.
DR STRING; 1283841.A0A084Q8G4; -.
DR HOGENOM; CLU_020880_3_0_1; -.
DR InParanoid; A0A084Q8G4; -.
DR OMA; ANSPWFA; -.
DR OrthoDB; 2404758at2759; -.
DR Proteomes; UP000028524; 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:UP000028524};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..518
FT /note="3-phytase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001779112"
FT ACT_SITE 80
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 69..398
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 262..276
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 518 AA; 56844 MW; 3B20C8DD7BC85E1B CRC64;
MSFATTACLL LAAAGAANAR AGSPLDPVQP VLLPDGALAK NPLAHLGGNG PWTVAPDVHG
ISTDVPDNCY VDQAAYVLRH GSRYPDAGAH SGWVDMARRF REYNFTASGP LSFFHSWDTP
LTHPDIQIAQ QSQTGYKELH DLGYTLRTRY PNLYEEGDNF YVWANNYTRV LQTAQMFVRG
YLGTNSSVVG NVVSVTARGV PAHLADTLAP SDMCPTFRDN SSPQTSVWQA TWLPGFIDRL
SRYIDGDLEL QNGQWNDFPY ICGFESQITG RMSPFCDTFT QEELNAYEYQ QDLRYYYGVG
PGADVSSKMM VPFLSALVDR FVEGPDAEGT NVDGGSFKLP KLLMSFLNDG QLNQLAAAVG
IFDEQEPLPT DRMPEDRLWR SSRISPMRGT IAFERLNCRV NGTATPTSTP SSTSLVFSTV
SGTPCIPRPT HLPGRNETFV RIRLNEAVYP VPSCQDGPGR SCRVSDYSRY VSEKFEAQGG
ADGFAELCNA TDPATPTRVL GASFFTDLSS AHLQIIRP
//
