ID A0A1F8AC73_9EURO Unreviewed; 457 AA.
AC A0A1F8AC73;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN ORFNames=ABOM_004119 {ECO:0000313|EMBL:OGM49293.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM49293.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM49293.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
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:OGM49293.1}.
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; LYCR01000010; OGM49293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8AC73; -.
DR STRING; 109264.A0A1F8AC73; -.
DR OrthoDB; 2404758at2759; -.
DR Proteomes; UP000179179; 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:UP000179179};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..457
FT /note="3-phytase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009534717"
FT ACT_SITE 62
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT ACT_SITE 321
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT DISULFID 51..370
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 235..249
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 394..402
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 457 AA; 50199 MW; 14BEFEEA5476AAED CRC64;
MGVTLRTLWL LGLSSAASAR AFEPLEHLGA NSPWFAGPNV NKIASTVPEE CSVDQAVYVV
RHGSRYPDPG AYQEWEGLHK AFQSAEYRAT GSLSFISDWS PVLRHPDQEI SQLYNLGADL
RFRYPTFYKD NTPFLLWAND YQRTIDSARL FARGYLGPNA SYGDVYIVDA DASSAAGNSL
ATSDQCPNFK DASGGDQIAE WQDIYLPPIT KRLNRKLSGN LTLTDDQVSL FPYLCGFETQ
ITGQVSPWCD VFTKKELLEY EYAQDLRYYY GTGPGVGKNM TVMLPVLQGV VNLLKEGPAA
TADKGNGTLQ LPPLVVAFTH DNQINELASI LGVFDDQKPL ASDEMDRDRI YVSSNVNPMR
GTIAFERLTC TSGGKSMANV RILLNDAVYP IPSCRSGPGS SCPVDQYAQY VAQKRKEYGS
FASVCGLPEK NITTAGADGA VTFFSDLTLP FLRVVKP
//
