XYNB_PHACH
ID XYNB_PHACH Reviewed; 290 AA.
AC B7SIW1;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 43.
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 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 [GENOMIC DNA], SUBCELLULAR LOCATION, IDENTIFICATION BY
RP MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=RP78;
RX PubMed=15278289; DOI=10.1007/s00294-004-0520-x;
RA Decelle B., Tsang A., Storms R.K.;
RT "Cloning, functional expression and characterization of three Phanerochaete
RT chrysosporium endo-1,4-beta-xylanases.";
RL Curr. Genet. 46:166-175(2004).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16348798; DOI=10.1128/aem.58.11.3466-3471.1992;
RA Dobozi M.S., Szakacs G., Bruschi C.V.;
RT "Xylanase Activity of Phanerochaete chrysosporium.";
RL Appl. Environ. Microbiol. 58:3466-3471(1992).
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. {ECO:0000269|PubMed:15278289,
CC ECO:0000269|PubMed:16348798}.
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:15278289,
CC ECO:0000269|PubMed:16348798};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.96 mg/ml for birchwood xylan {ECO:0000269|PubMed:15278289};
CC pH dependence:
CC Optimum pH is 4.5. {ECO:0000269|PubMed:15278289};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:15278289};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15278289}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; EU302793; ABZ88798.1; -; Genomic_DNA.
DR AlphaFoldDB; B7SIW1; -.
DR SMR; B7SIW1; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11B_PHACH; -.
DR VEuPathDB; FungiDB:AGR57_6406; -.
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; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..290
FT /note="Endo-1,4-beta-xylanase B"
FT /id="PRO_5000419220"
FT DOMAIN 34..222
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT DOMAIN 255..290
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 223..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 118
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 209
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 290 AA; 30466 MW; 6D0583921B4F6580 CRC64;
MVSFNSLLVA VSAATCALAF PFEFHNGTHV FPRQSTPAGT GTNNGYFYSF WTDGGGSVTY
NNGPAGEYSV TWSNADNFVA GKGWNPGSAQ AISFTANYQP NGNSYLSVYG WSTNPLVEYY
ILEDFGTYNP AVSLTHKGTL TSDGATYDVY EGTRVNEPSI QGTATFNQYW SIRSSKRSSG
TVTTANHFAA WKQLGLPLGT FNYQIVATEG YQSSGSSTVT VNPAGGVTSP IAPTGPSSVS
TTPSGPSSSP SPVGTCSALY GQCGGQGWTG PTCCSSGTCK FSNNWYSQCL
