ID   A0A135S952_9PEZI        Unreviewed;       389 AA.
AC   A0A135S952;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:KXH32444.1};
GN   ORFNames=CNYM01_00992 {ECO:0000313|EMBL:KXH32444.1};
OS   Colletotrichum nymphaeae SA-01.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH32444.1, ECO:0000313|Proteomes:UP000070054};
RN   [1] {ECO:0000313|EMBL:KXH32444.1, ECO:0000313|Proteomes:UP000070054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA-01 {ECO:0000313|EMBL:KXH32444.1,
RC   ECO:0000313|Proteomes:UP000070054};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:KXH32444.1}.
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DR   EMBL; JEMN01001582; KXH32444.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135S952; -.
DR   Proteomes; UP000070054; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd18833; GH43_PcXyl-like; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR   PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|RuleBase:RU361187};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..389
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007801949"
FT   ACT_SITE        34
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        209
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            156
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ   SEQUENCE   389 AA;  42693 MW;  BFD5724C11861502 CRC64;
     MKSGLLALAI ALFGVAQAEN STFQNPIISG FNPDPSCIFV PELNNTFFCA TSSFLVFPGL
     PIHTSRDLVH WKHVSNAFSR ADQLPGLAFL PKATSGIYAP TLRFHEGIFY LLCTLVNQQL
     PRTNDSRWDN FILTSTDPYS SDSWSDPVHF SFPGFDPSPF WDDDGKTYVS GAHTAAYYPG
     IMHAPLDLET GEIGDIIMPW NGTGGRSPEA PHIWKRDGWY YLLLAEGGTR ENHMVTMARS
     KSLEGPYDPA PANPLLTSAN DTTSYFQAVG HADLFQDSDG NWWSVALAVR AGGTYGQDPG
     AYFGNLPMGR ETVLTPVTWE RDKFPVFTPV TGNVSGWPLP AKSIPEKGEG QLSDADDVIT
     FPPGSSLPIH FIHWRLPKAR NYAVSPPGH
//