ID A0A1V6U7S4_9EURO Unreviewed; 353 AA.
AC A0A1V6U7S4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Beta-xylosidase C-terminal Concanavalin A-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENCOP_c017G05119 {ECO:0000313|EMBL:OQE34526.1};
OS Penicillium coprophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE34526.1, ECO:0000313|Proteomes:UP000191500};
RN [1] {ECO:0000313|Proteomes:UP000191500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31321 {ECO:0000313|Proteomes:UP000191500};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE34526.1}.
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DR EMBL; MDDG01000017; OQE34526.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6U7S4; -.
DR STRING; 36646.A0A1V6U7S4; -.
DR OrthoDB; 1943490at2759; -.
DR Proteomes; UP000191500; 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; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000191500}.
FT SITE 133
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 353 AA; 39760 MW; FCAB96300B4149D6 CRC64;
MSKPLINHIY TADPSAHVFN NKLYIYPSHD RETDIAFNDN GDQYDMADYH VLSMDTITGP
VTDHGVVLRD KDIPWVSKQL WAPDAATKNN KFYLFFPARD QKGIFRIGVA VSDAPDGPFV
PQDDYIKGSY SIDPAVFVDE EAGGEAYLYV GGIWGGQLQC WVEGKDIENG EWVDGDEGGV
DGKKKRLVFD ESMSGPQEPS GEGVRALCPR VARLSDDMTS LAESVKEVVI LAPETGEPLL
ADDHERRFFE AAWVHRYNGT YYFSYSTGDT HFLAYATGDS PYGPFTYRGR ILDPVLGWTT
HHSIVEFQEK WYLFYHDCEL SKGVDHLRSV KVREIVYDDE GAIRLAEKQT AVE
//
