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 27-MAR-2024, entry version 108. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 RefSeq; XP_001388522.1; XM_001388485.2. DR AlphaFoldDB; P55330; -. DR SMR; P55330; -. DR CAZy; GH11; Glycoside Hydrolase Family 11. DR PaxDb; 5061-CADANGAP00000070; -. DR EnsemblFungi; CAK43456; CAK43456; An01g00780. DR GeneID; 4978152; -. DR VEuPathDB; FungiDB:An01g00780; -. DR VEuPathDB; FungiDB:ASPNIDRAFT2_1101058; -. DR VEuPathDB; FungiDB:ATCC64974_22790; -. DR VEuPathDB; FungiDB:M747DRAFT_331912; -. DR eggNOG; ENOG502RXA7; Eukaryota. DR OrthoDB; 1778490at2759; -. 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 PANTHER; PTHR46828; ENDO-1,4-BETA-XYLANASE A-RELATED; 1. DR PANTHER; PTHR46828:SF2; ENDO-1,4-BETA-XYLANASE A-RELATED; 1. DR Pfam; PF00457; Glyco_hydro_11; 1. DR PRINTS; PR00911; GLHYDRLASE11. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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 //