ID A0A194VJ31_9PEZI Unreviewed; 359 AA.
AC A0A194VJ31;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Xylosidase/arabinosidase {ECO:0000313|EMBL:KUI64151.1};
GN ORFNames=VM1G_10927 {ECO:0000313|EMBL:KUI64151.1};
OS Valsa mali.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI64151.1};
RN [1] {ECO:0000313|EMBL:KUI64151.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-8 {ECO:0000313|EMBL:KUI64151.1};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-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}.
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DR EMBL; KN796121; KUI64151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194VJ31; -.
DR OrthoDB; 5470935at2759; -.
DR Proteomes; UP000078559; 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:UniProtKB-KW.
DR CDD; cd18619; GH43_CoXyl43_like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187}.
FT SITE 146
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 359 AA; 39974 MW; CCEF6E8FB6C27E03 CRC64;
MPPLITHLYT ADPSAHVFNG KIYIYPSHDE DTGAESNDNG DQYDMADYHV FSIDCSPDPN
IARPATSPAP TVTDHGVVLR LADVPWASKQ LWAPDAAHNP RDGRYYLFFP ARDKDGIFRI
GVAAGDKPEG PFTPEENYIP GTYSIDPAVL VDDDDDDEEE EEEEKKQAYL YFGGIWGGQL
QCYQKGNDVF DPSWTGPKEP SGAGVHALGP RVARLSGDMR SLASEVREIE ILDPETGARI
AADDHERRFF EAAWCHKRRG KYYFSYSTGD THFLCYAVGD GPMGPFTYGG RLLEPVLGWT
THHSVVEFPV GSDRWWLFYH DCELSGGVSH LRSVKVRELW YDGDRIVGGK PTSSSSQGD
//