ID A0A066XAS3_COLSU Unreviewed; 517 AA.
AC A0A066XAS3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=3-phytase {ECO:0000256|ARBA:ARBA00012632};
DE EC=3.1.3.8 {ECO:0000256|ARBA:ARBA00012632};
GN ORFNames=CSUB01_09179 {ECO:0000313|EMBL:KDN66263.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN66263.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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:KDN66263.1}.
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DR EMBL; JMSE01000949; KDN66263.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XAS3; -.
DR STRING; 1173701.A0A066XAS3; -.
DR eggNOG; KOG1382; Eukaryota.
DR HOGENOM; CLU_020880_3_0_1; -.
DR OMA; ANSPWFA; -.
DR OrthoDB; 2404758at2759; -.
DR Proteomes; UP000027238; 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:UP000027238};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..517
FT /note="3-phytase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001633763"
FT ACT_SITE 78
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT ACT_SITE 351
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT DISULFID 67..400
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 264..278
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 456..464
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 517 AA; 56684 MW; 9287641CDE6477D4 CRC64;
MAAVKFGIIC LATTLVEGSS RFLAPVQDIN LPASDSAAHP LEHLGANGPW FAGPNVNDIS
SDIPENCYVD QAAYVLRHGS RYPDPGAYNG WVSMQQRPMQ FQAGNYTASG SLSFLPKWRT
ALTNPSSQIS NLSPTGYKEI HDLGYTLRTR YPDLYTEGEN FMVWANNYSR VIQTAQLFVR
GFLGTNATLL GDVISVTSRG FPGGIGDSLA PSDMCPTFKD SEGDDAVTQW NSIYIPPIQA
RLQALIEGNL TLTPGDISQI PYLCGYESQI TGRLSPWCDI FTDEEFLQYE YFQDLRYYYG
VGPGTDIPQK MMTPFLNSLM GILEEGPSVT GKREDGSSFN LPKLIMSFLN DGQLNQLITA
SGVFDEQEPL SSTKKDDDRQ YVSSRFTTMR GTIAFERLNC VVAGNGTSAN AIRQAQPPRP
IRRFGSAQAP TQAQGSNNAT YVRIRLNDAV YPVPSCRSGP GSSCLLKDYK QYVATKLEAQ
GNWIENCNVT TPGAPKEVKG ASFFTDLSSP WLSHVAP
//
