ID A1CXF7_NEOFI Unreviewed; 462 AA.
AC A1CXF7;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN ORFNames=NFIA_108020 {ECO:0000313|EMBL:EAW25309.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW25309.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; DS027685; EAW25309.1; -; Genomic_DNA.
DR RefSeq; XP_001267206.1; XM_001267205.1.
DR AlphaFoldDB; A1CXF7; -.
DR STRING; 331117.A1CXF7; -.
DR EnsemblFungi; EAW25309; EAW25309; NFIA_108020.
DR GeneID; 4593546; -.
DR KEGG; nfi:NFIA_108020; -.
DR VEuPathDB; FungiDB:NFIA_108020; -.
DR eggNOG; KOG1382; Eukaryota.
DR HOGENOM; CLU_020880_3_1_1; -.
DR OMA; RGRSDWC; -.
DR OrthoDB; 2404758at2759; -.
DR Proteomes; UP000006702; 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; 3.
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:SF18; ACID PHOSPHATASE PHO11-RELATED; 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.
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:UP000006702};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..462
FT /note="3-phytase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002633863"
FT ACT_SITE 68
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT ACT_SITE 328
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT DISULFID 57..377
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 403..411
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 462 AA; 51706 MW; E0A3C5622FDC5DC2 CRC64;
MVRRYAQLLV LIPATTATLL FSQQTLDGNN ILKHNGAMGP YVDRSNYGIN RAPPAGCSVD
QVIMIKRHGE RYPLASEGPK IEKALQKVKK AVFDEPHADG DLDFVKNWTY FVPSSCYYDK
ETTTGPYNGI QDAYKHGMDA RNRYGHLWDE ETIVPLFASD AGRIVDTARM FGEGFFGDDE
YKTKAAINII PESARQGANA LSRTCHARDH HAQRICDAWP QSLPQLELAT QRLNGQYLGL
DLTSTDIFWL MTMSSYEPSV RGHSDWTGVF TMDEWVSFGY IWDLHFYYCA GPGNKMMRPV
GSLYVNASLA LLEQGPSSGT LFFNFAHDTD ITPIIGALGI LNPPEDLPTD RVSFGHSWLS
SELVPMGGHL TMERLSCNAT AIVPAGTYVR VVLNEAVVPF RACQSGPGYS CPLQEYASIV
RQDLPDYVLE CEIPESDPQH LDFWWDYSTA TTDNYRDETK CD
//