XYNB_ASPNG
ID XYNB_ASPNG Reviewed; 225 AA.
AC P55330; B1A5N7; C0LVA6; C6F1T2; Q12557; Q8TG22;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 101.
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 AltName: Full=Endo-1,4-beta-xylanase G1;
DE Short=Xylanase G1;
DE AltName: Full=Endo-1,4-beta-xylanase II;
DE Short=Xylanase II;
DE Flags: Precursor;
GN Name=xlnB; Synonyms=xyn2, xynB, xynG1;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 4066 / RIB 1061;
RA Ito K.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gu S., Sun J., Xu Z., Li W., Zhao H.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zhu L., Liu W., Dong Z., Yu W.;
RT "High-level expression of xylanase B of Aspergillus niger in Pichia
RT pastoris.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND ACTIVITY REGULATION.
RX DOI=10.1016/j.enzmictec.2006.02.014;
RA Deng P., Li D., Cao Y., Lu W., Wang C.;
RT "Cloning of a gene encoding an acidophilic endo-beta-1,4-xylanase obtained
RT from Aspergillus niger CGMCC1067 and constitutive expression in Pichia
RT pastoris.";
RL Enzyme Microb. Technol. 39:1096-1102(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=IBT-90;
RX DOI=10.1016/j.enzmictec.2005.12.003;
RA Korona B., Korona D., Bielecki S.;
RT "Efficient expression and secretion of two co-produced xylanases from
RT Aspergillus niger in Pichia pastoris directed by their native signal
RT peptides and the Saccharomyces cerevisiae a-mating factor.";
RL Enzyme Microb. Technol. 39:683-689(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Su Y., Bai J., Chen G.;
RT "Isolation and identification of xynB from Aspergillus niger.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=F19;
RA Cui L., Zhang Z., Zhu M., Wang C.;
RT "Cloning, expression and characterization of the xylanase B from
RT Aspergillus niger F19 in Escherichia coli.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DMS1957;
RA Nguyen S.L.T., Quyen D.T.;
RT "Gene cloning, sequencing, expression and characterization of a xylanase
RT gene from Aspergillus niger DMS1957.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SCTCC 400264;
RA Yi X., Qiao D., Cao Y.;
RT "Expression of Xylanase Gene xynB from Aspergillus niger in Escherichia
RT coli and Characterization of Its Recombinant Xylanase.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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:0000250, ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
CC -!- ACTIVITY REGULATION: Metal ions, copper, iron and N-bromosuccinimide
CC decrease enzyme activity. Manganese, calcium, L-tryptophan, beta-
CC mercaptoethanol, L-cysteine and dithiodipyridine stimulate the enzyme
CC activity. {ECO:0000269|Ref.4}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.0. Retains about 76 percent of its activity after
CC being incubated at pH 2.0 for 30 min at 37 degrees Celsius.
CC {ECO:0000269|Ref.4, ECO:0000269|Ref.5};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius. Displays about 95 percent
CC of peak activity in the temperature range from 37 to 41 degrees
CC Celsius. {ECO:0000269|Ref.4, ECO:0000269|Ref.5};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; D38071; BAA07265.1; -; Genomic_DNA.
DR EMBL; AF490982; AAM08362.1; -; mRNA.
DR EMBL; AY126481; AAM95167.1; -; Genomic_DNA.
DR EMBL; DQ174549; ABA00146.1; -; Genomic_DNA.
DR EMBL; AY536639; AAS46914.1; -; mRNA.
DR EMBL; EU423881; ACA24724.1; -; Genomic_DNA.
DR EMBL; EU430370; ACA51680.1; -; mRNA.
DR EMBL; EU848305; ACJ26382.1; -; mRNA.
DR EMBL; FJ772090; ACN89393.1; -; mRNA.
DR AlphaFoldDB; P55330; -.
DR SMR; P55330; -.
DR STRING; 5061.CADANGAP00000070; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR VEuPathDB; FungiDB:An01g00780; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1101058; -.
DR VEuPathDB; FungiDB:ATCC64974_22790; -.
DR VEuPathDB; FungiDB:M747DRAFT_331912; -.
DR eggNOG; ENOG502RXA7; Eukaryota.
DR UniPathway; UPA00114; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IDA:UniProtKB.
DR GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.120.180; -; 1.
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; PF00457; Glyco_hydro_11; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SUPFAM; SSF49899; SSF49899; 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..18
FT /evidence="ECO:0000255"
FT PROPEP 19..37
FT /id="PRO_0000007993"
FT CHAIN 38..225
FT /note="Endo-1,4-beta-xylanase B"
FT /id="PRO_0000007994"
FT DOMAIN 37..225
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 121
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT CONFLICT 16
FT /note="A -> V (in Ref. 2; AAM08362, 3; AAM95167, 4;
FT ABA00146, 5; AAS46914 and 7; ACA51680)"
FT /evidence="ECO:0000305"
FT CONFLICT 25..26
FT /note="AQ -> VE (in Ref. 2; AAM08362, 3; AAM95167, 4;
FT ABA00146, 5; AAS46914 and 7; ACA51680)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="M -> K (in Ref. 2; AAM08362, 3; AAM95167, 4;
FT ABA00146, 5; AAS46914 and 7; ACA51680)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="A -> S (in Ref. 2; AAM08362, 3; AAM95167, 4;
FT ABA00146, 5; AAS46914 and 7; ACA51680)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="S -> P (in Ref. 8; ACJ26382)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="D -> V (in Ref. 6; ACA24724)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 225 AA; 24057 MW; C4B8BB007AB2B8FD CRC64;
MLTKNLLLCF AAAKAALAVP HDSVAQRSDA LHMLSERSTP SSTGENNGFY YSFWTDGGGD
VTYTNGDAGA YTVEWSNVGN FVGGKGWNPG SAQDITYSGT FTPSGNGYLS VYGWTTDPLI
EYYIVESYGD YNPGSGGTYK GTVTSDGSVY DIYTATRTNA ASIQGTATFT QYWSVRQNKR
VGGTVTTSNH FNAWAKLGMN LGTHNYQIVA TEGYQSSGSS SITVQ
