ID B8MHA0_TALSN Unreviewed; 512 AA.
AC B8MHA0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN ORFNames=TSTA_021360 {ECO:0000313|EMBL:EED17079.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED17079.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EQ962656; EED17079.1; -; Genomic_DNA.
DR RefSeq; XP_002484313.1; XM_002484268.1.
DR AlphaFoldDB; B8MHA0; -.
DR STRING; 441959.B8MHA0; -.
DR GeneID; 8109393; -.
DR VEuPathDB; FungiDB:TSTA_021360; -.
DR eggNOG; KOG1382; Eukaryota.
DR HOGENOM; CLU_020880_3_0_1; -.
DR InParanoid; B8MHA0; -.
DR OMA; ANSPWFA; -.
DR OrthoDB; 2404758at2759; -.
DR PhylomeDB; B8MHA0; -.
DR Proteomes; UP000001745; 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:UP000001745};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..512
FT /note="3-phytase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002875113"
FT ACT_SITE 81
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT ACT_SITE 364
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT DISULFID 70..413
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 276..290
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 450..458
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 512 AA; 55526 MW; 3A3CA1C80C555341 CRC64;
MASIKSITAS ILLFSALSTA SVGQILAPSD DIVFAASASA KDPLAWAGAN SPYRAGPNVY
GISNEVPDGC SVKQAAYIVR HGSRFPDSGA YAGWVDLRNR IQAAKTAGNL TARGSLSFIP
NWKTVLTNPT LQISQESMTG YNEGHNLGYQ LRARYPNFYE DGNQFYVWAN QYASPINESR
VVQTAKAFMQ GYLAEFADAY GTIVSVNSTG SVNAIGNSLG PSDACPAFAA GPSGSDFNNA
TDYEAIWTPK VLKRINSLVD GIEFTQSDIL SMPYLCGFES QITGRLSPWC GVFTDEELEF
YEYSQDLHYY YGIGPGSTTP TNKLFLPFLD SLITLLKAGP DQQGKGVNGT KFDIPKLLMA
FLNDNQIAEL TAGMGIFDAQ ENLPIDRILK DRIYNVANFI TMRGTVTFEV LNCTSSSPIF
EYDSELCASE TYSDYIRILL NDAAYILPHC HDGPGGSCLL SEYASFISKR SAAAGNFNEY
CNVTKAGHPV TVGGASFFSD LTLDFLEFVA PH
//
