ID A0A318ZWF2_ASPLB Unreviewed; 548 AA.
AC A0A318ZWF2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN ORFNames=BO96DRAFT_469831 {ECO:0000313|EMBL:PYH51641.1};
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH51641.1, ECO:0000313|Proteomes:UP000247441};
RN [1] {ECO:0000313|EMBL:PYH51641.1, ECO:0000313|Proteomes:UP000247441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH51641.1,
RC ECO:0000313|Proteomes:UP000247441};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; KZ821377; PYH51641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318ZWF2; -.
DR OrthoDB; 2721627at2759; -.
DR Proteomes; UP000247441; 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 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 SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..548
FT /note="3-phytase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016272059"
SQ SEQUENCE 548 AA; 62679 MW; 6EE892034AA22A76 CRC64;
MRSRIYWAIL FLLLVSCVSA NDQYVMGVAP TTTEPEWFKT RPQSFQGYTA TGAAPFLAQT
NPAPFGNPAT YTANHPLETS QPIRGGKDRN IFHHMGILSP YYPRADGFGV DEFPRPKGSN
ITQMHMLHRH GSRYPNKDEA HGAVFKDELS FIHDWTYSLG ADMLTTRGRE DLLESGILNF
YNYGHLYTPG TKIVARTTTQ DRMLKSAENF LAGFFHLDWD EHVNLLAMIE EKNFNSSLQA
KNACPNAMKI SFDDYVSDTV TKWKTHYLSH RTHHLNYLST DYHWTSNDSF NAQTLCAYET
VALGYSPWCS LFTFPEWEGF SYTYDLTFGG NAGFQCPISR AMGITWVQEF LARVENRSFS
TPGSSSAANL TLNTNPVTFP TNQSLYFDFA HDKILLGVLT AFGLRQFADL PFPDYTDQYF
MDVFPPRHHA FQTAKLIPFA GRLNIEIIRA PHKINPRRSH HDRHQDTYMK HTAETEYVHF
LLNQRTVPLH KSLPECSFRS DGWCELDAFL RAQKDSLRKA EYDFSCVGEW DLGEFGDVWD
GVPVLRGE
//
