XYNB_PENOX
ID XYNB_PENOX Reviewed; 310 AA.
AC E7EF85;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Endo-1,4-beta-xylanase B;
DE Short=Xylanase B;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase B;
DE Flags: Precursor;
GN Name=xynB;
OS Penicillium oxalicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=69781;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION,
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=B3-11-2;
RX PubMed=23412069; DOI=10.4014/jmb.1208.08030;
RA Wang J., Mai G., Liu G., Yu S.;
RT "Molecular cloning and heterologous expression of an acid-stable
RT endoxylanase gene from Penicillium oxalicum in Trichoderma reesei.";
RL J. Microbiol. Biotechnol. 23:251-259(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=GZ-2;
RA Liao H., Xu C., Tan S., Shen Q., Xu Y.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX PubMed=22940308; DOI=10.1016/j.biortech.2012.07.051;
RA Liao H., Xu C., Tan S., Wei Z., Ling N., Yu G., Raza W., Zhang R., Shen Q.,
RA Xu Y.;
RT "Production and characterization of acidophilic xylanolytic enzymes from
RT Penicillium oxalicum GZ-2.";
RL Bioresour. Technol. 123:117-124(2012).
CC -!- FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a
CC major structural heterogeneous polysaccharide found in plant biomass
CC representing the second most abundant polysaccharide in the biosphere,
CC after cellulose. Hydrolyzes birchwood xylan, beechwood xylan, and oat
CC spelt xylan to produce short-chain xylooligosaccharides, xylopentaose,
CC xylotriose, and xylobiose as the main products.
CC {ECO:0000269|PubMed:22940308, ECO:0000269|PubMed:23412069}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000269|PubMed:22940308,
CC ECO:0000269|PubMed:23412069};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 mg/ml for birchwood xylan {ECO:0000269|PubMed:22940308,
CC ECO:0000269|PubMed:23412069};
CC KM=4.6 mg/ml for beechwood xylan {ECO:0000269|PubMed:22940308,
CC ECO:0000269|PubMed:23412069};
CC KM=11.3 mg/ml for oat spelt xylan {ECO:0000269|PubMed:22940308,
CC ECO:0000269|PubMed:23412069};
CC Vmax=2 umol/min/mg enzyme toward birchwood xylan
CC {ECO:0000269|PubMed:22940308, ECO:0000269|PubMed:23412069};
CC Vmax=2 umol/min/mg enzyme toward beechwood xylan
CC {ECO:0000269|PubMed:22940308, ECO:0000269|PubMed:23412069};
CC Vmax=2.5 umol/min/mg enzyme toward oat spelt xylan
CC {ECO:0000269|PubMed:22940308, ECO:0000269|PubMed:23412069};
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:22940308,
CC ECO:0000269|PubMed:23412069};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:22940308, ECO:0000269|PubMed:23412069};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23412069}.
CC -!- INDUCTION: Induced by soluble xylo-oligosaccharides, with beechwood
CC xylan being the best inducer. {ECO:0000269|PubMed:22940308}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; HQ680966; ADV31286.1; -; Genomic_DNA.
DR EMBL; KF233758; AGW24301.1; -; mRNA.
DR AlphaFoldDB; E7EF85; -.
DR SMR; E7EF85; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11A_PENOX; -.
DR BRENDA; 3.2.1.8; 4629.
DR UniPathway; UPA00114; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.120.180; -; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR018208; GH11_AS_1.
DR InterPro; IPR033119; GH11_AS_2.
DR InterPro; IPR033123; GH11_dom.
DR InterPro; IPR001137; Glyco_hydro_11.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00457; Glyco_hydro_11; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00776; GH11_1; 1.
DR PROSITE; PS00777; GH11_2; 1.
DR PROSITE; PS51761; GH11_3; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..310
FT /note="Endo-1,4-beta-xylanase B"
FT /id="PRO_0000429615"
FT DOMAIN 33..223
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT DOMAIN 275..310
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 218..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
SQ SEQUENCE 310 AA; 31282 MW; 0EE37FBE5422BF73 CRC64;
MISLSSVAIA LTTVVGALAL PSDQSVNLAA RQAITSSQTG TNNGYYYSFW TNGAGSVSYS
NGAAGQFSVN WANQGGGDFT CGKGWNPGKA QDISFSGTFT PNGNAYLSIY GWTTGPLVEY
YILENFGSYN PGNGMTHVGT LTSDGSDYDI YKHTQVNQPS IVGTSTFDQY WSIRKNKRSS
GTVTTANHFS AWASHGMNLG SHNYQILSVE GYQSSGSASM TVSAGSSSSG GSGSGSGSGS
GSGSGSGSQT TTAGSSTGTG TGSGSGSGSG GSGGNCAAQW GQCGGQGWNG PTCCSSGTCK
ASNQWYSQCL
