ID S0END3_GIBF5 Unreviewed; 485 AA.
AC S0END3;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, 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=FFUJ_11523 {ECO:0000313|EMBL:CCT75499.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT75499.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; HF679033; CCT75499.1; -; Genomic_DNA.
DR AlphaFoldDB; S0END3; -.
DR STRING; 1279085.S0END3; -.
DR EnsemblFungi; CCT75499; CCT75499; FFUJ_11523.
DR VEuPathDB; FungiDB:FFUJ_11523; -.
DR HOGENOM; CLU_020880_3_0_1; -.
DR OrthoDB; 2404758at2759; -.
DR Proteomes; UP000016800; Chromosome 11.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000016800};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..485
FT /note="3-phytase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004496266"
FT ACT_SITE 81
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 70..398
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 262..276
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 424..432
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 485 AA; 53696 MW; 09B1FD885D601971 CRC64;
MRGPFIAVAL LGSACSARNA GVGASLDPVQ AVLLPDGASA KNPLAHVGAN GPWHIGEELT
GISSEVPEGC QVDQAAYVSR HGSRYPDQGA HNGWLEMARR FRESKYTATG PLSFIHTWES
PLTNPDIQIA QLSKTGYKEL FDMGYTLRTR YPDLYQEGED FIVWANNYTR VLQTAKLFLH
GFLGTNSSLG TVVSVTGKGV PSHLGDTLAP SDMCPTFIDD SSKQQDEWRQ RWLPGFKKRL
SRYIKGDLQL DDSTWNDFPY ICGFESQIKG KLSPFCDTFT QKELEAYEYQ QDLRYYYGVG
PATKVASKMM VPFLESLIER FVAGPDTTGK DFDGKPFKLP KILMSFLNDG QLNELAVATG
VFDKQAPLPL DRIPKDRIWR SSNISPMRGT IAFERLSCGS NKAYGSKKFV RILINDVVYP
VPSCRDGPGK SCSLSKYSKF TKDRLRKNGN FAKLCNATDP ATPSKVLGAS FFTNLAQSHL
QAVEP
//
