XYL5_PHACH
ID XYL5_PHACH Reviewed; 476 AA.
AC W8QRE4;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 2.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=Beta-xylosidase {ECO:0000303|PubMed:25300189};
DE EC=3.2.1.37 {ECO:0000269|PubMed:25300189};
DE AltName: Full=1,4-beta-D-xylan xylohydrolase;
DE AltName: Full=Xylan 1,4-beta-xylosidase;
GN Name=Xyl5 {ECO:0000303|PubMed:25300189};
OS Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerodontia.
OX NCBI_TaxID=2822231;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM
RC F-1767;
RX PubMed=25300189; DOI=10.1016/j.jbiosc.2014.09.012;
RA Huy N.D., Nguyen C.L., Seo J.W., Kim D.H., Park S.M.;
RT "Putative endoglucanase PcGH5 from Phanerochaete chrysosporium is a beta-
RT xylosidase that cleaves xylans in synergistic action with endo-xylanase.";
RL J. Biosci. Bioeng. 119:416-420(2015).
CC -!- FUNCTION: Catalyzes the hydrolysis of xylo-oligomers to xylose units
CC and plays an important role in xylan degradation. Can also perform the
CC transglycosylation of xylose and alcohol. Has no endoglucanase
CC activity. {ECO:0000269|PubMed:25300189}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-
CC xylose residues from the non-reducing termini.; EC=3.2.1.37;
CC Evidence={ECO:0000269|PubMed:25300189};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5. Stable from pH 3 to pH 8.
CC {ECO:0000269|PubMed:25300189};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:25300189};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25300189}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; KF977410; AHL69750.2; -; mRNA.
DR EMBL; KJ624721; AIA81045.1; -; mRNA.
DR AlphaFoldDB; W8QRE4; -.
DR SMR; W8QRE4; -.
DR VEuPathDB; FungiDB:AGR57_14021; -.
DR BRENDA; 3.2.1.37; 1380.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosidase; Hydrolase; Secreted.
FT CHAIN 1..476
FT /note="Beta-xylosidase"
FT /id="PRO_0000438825"
FT ACT_SITE 188
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q45070"
FT ACT_SITE 292
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q45070"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 476 AA; 55475 MW; 8C8FC70648F725C4 CRC64;
MAYLKVSGTK IVDKDGNEVI LRGAGLGGWM NMENFITGYP GCEFQIRAAL ADVVGQEKSE
FFFDKFLEYF FTDADAAFFK SLGLNCIRLP FNYRHFEDDM NPRVLKPEGF KHLDRVIDIC
AKHGIYTVLD LHTAPGGQNT DWHSDAGTHI AKFWEHKDFQ DRVIWLWEEL AQHYRDNTWI
AGYNPLNEPT DPYQTRLIAW YDRVYAAIRK HDPHHALFLD GNTFASDFSH FGDAEKRWEN
TAYAIHDYSV FGFPAAPEPY VSSEAQRRRL RRSYEKKREW MDARGLCVWN GEFGPVYARR
EYEGDLTDSI NEERYRVLKD QLEIYNKDRL SWSIWLYKDI GFQGMVHVSR DTPYMTLFRD
FLAKKHRLAI DAWGADDSAV RHVYQPLIDL IKQEVKPEHQ ELYPAPVWKL SDRVGRLARN
ILVSEFLVRE WAEHFRGKST EELDAIAKSF AFENCLHRDG LNKVLTDNAS LVAQGA
