ID S8AZ08_PENO1 Unreviewed; 521 AA.
AC S8AZ08;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Putative beta-xylosidase {ECO:0000313|EMBL:EPS27222.1};
GN ORFNames=PDE_02165 {ECO:0000313|EMBL:EPS27222.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS27222.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS27222.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; KB644410; EPS27222.1; -; Genomic_DNA.
DR AlphaFoldDB; S8AZ08; -.
DR STRING; 933388.S8AZ08; -.
DR eggNOG; ENOG502QQH8; Eukaryota.
DR HOGENOM; CLU_016508_2_0_1; -.
DR OrthoDB; 1891044at2759; -.
DR PhylomeDB; S8AZ08; -.
DR Proteomes; UP000019376; 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; cd18617; GH43_XynB-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
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; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
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:UP000019376}.
FT DOMAIN 329..520
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 14
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 193
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 132
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 521 AA; 59136 MW; D9E7D60D2E6705EA CRC64;
MTYTNPVIPG FNPDPSIVRV NEDYFLVTSS FEYFPGAPIY HSRDLIQWKL VGHALTRLSQ
LQIHTPEPGG GVWATTIRYH DGEFYILAAS FQRYRPQEDD RVWPRGFYVK TKDIWDDGSW
SDPVYFDQVG FDQDIFWDDD GTVYLSSTYR KLLPTPGVKL KDFAIHISTV DLATGRSTSA
PRLIRESTSG VAEGSHIFKR GRYYYLFTAE GGTEGGHCEW VSRSEAGPFG PWTLGPKNPL
WRNGTDDEVQ NTGHLDLVED VSGNWWAVLL AVRPVRKENG WEDSVFGRET FLVPVEWEND
WPIVNRGNKI TLQSEGPGLY AHESPVVWRD DFTSQTLSIG WYRKNTPLSV DYSLSERLHH
LRLHGGPYTL CVPASPTMFL RKQTHQVCTW ETRVSFHPSS EHTEAGTVLW WNYFTHSTIG
IRKRGPHRII RFQPSEGESI EMVLDSANDM ILLIECGKEY RFGYRDAANA EIIWVGAVSN
NAATRAPPVG APFTGMMLGL YAFGDRQPCQ APADFAYAQF A
//
