ID T0JR99_COLGC Unreviewed; 515 AA.
AC T0JR99;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN ORFNames=CGLO_15302 {ECO:0000313|EMBL:EQB45777.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB45777.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000032};
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:EQB45777.1}.
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DR EMBL; AMYD01003644; EQB45777.1; -; Genomic_DNA.
DR AlphaFoldDB; T0JR99; -.
DR STRING; 1237896.T0JR99; -.
DR eggNOG; KOG3720; Eukaryota.
DR HOGENOM; CLU_030431_3_1_1; -.
DR OMA; SWPPFTS; -.
DR OrthoDB; 5486499at2759; -.
DR Proteomes; UP000015530; 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; PTHR11567:SF110; ACID PHOSPHATASE 1, ISOFORM B; 1.
DR PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000015530}.
FT REGION 415..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 57231 MW; 7ED6AB3F0B5639BB CRC64;
MTTLEPRNPY TDAELRQLYP PQLKLQLVQI LLRHGERTPV TPRFQETGLP PYWPYCRVVR
HLRSAVLDPD TGEYSYLDWK RRLETFNPAD DSPIIAAGPN AELDDICDHG MLTDRGRETT
RNLGRRFRNL YVDRLGFLPA DLTNADSLYL RSTPVPRALE SLQQALTGLY PTQNRAPDLP
TLAIITRLQP DETLFPNDGM CRRFAVLSRA FAQRTADRWN ETPEIEYLNK KLGKWMPPGS
RVAVDSRPRL SGVMDSINAT RAHGPQTKLP SEFYDAKVIS IIEKIGVEEW YSGYKESQEY
RTLGIGGLMG DVVARMVGSV EHTPADGDYE IKNSGAAPHP VRFGMSGCHD TTLAGVLSSL
GAFGNDKWPP FTSHIAIELF RDSKVPAVET STTVPAAAAP QTGSWFNSWF SFGRSSTPSP
GTAPPGIGRK PTSDLTEAEK SQLDGYYVRL RYNDEPVTIP GCKPTGSHLE GDESFCTLAA
FKSIVDKYTP KNWKQQCRAN LDAPAIPANP EPAGY
//
