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Database: UniProt
Entry: P55330
LinkDB: P55330
Original site: P55330 
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   10-APR-2019, entry version 94.
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.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IFO 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
RP   PROPERTIES, 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
RT   obtained from Aspergillus niger CGMCC1067 and constitutive expression
RT   in Pichia pastoris.";
RL   Enzyme Microb. Technol. 39:1096-1102(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP   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
RT   xylanase 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
RT   Escherichia 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
CC       xylan, a major structural heterogeneous polysaccharide found in
CC       plant biomass representing the second most abundant polysaccharide
CC       in the biosphere, after cellulose. {ECO:0000250,
CC       ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8;
CC   -!- ACTIVITY REGULATION: Metal ions, copper, iron and N-
CC       bromosuccinimide decrease enzyme activity. Manganese, calcium, L-
CC       tryptophan, beta-mercaptoethanol, L-cysteine and dithiodipyridine
CC       stimulate the enzyme activity. {ECO:0000269|Ref.4}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.0. Retains about 76 percent of its activity
CC         after being incubated at pH 2.0 for 30 min at 37 degrees
CC         Celsius. {ECO:0000269|Ref.4, ECO:0000269|Ref.5};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius. Displays about 95
CC         percent of peak activity in the temperature range from 37 to 41
CC         degrees 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)
CC       family. {ECO:0000305}.
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   ProteinModelPortal; P55330; -.
DR   SMR; P55330; -.
DR   STRING; 5061.CADANGAP00000070; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   eggNOG; ENOG410IHTC; Eukaryota.
DR   eggNOG; ENOG410YH6C; LUCA.
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       {ECO:0000255}.
FT   PROPEP       19     37
FT                                /FTId=PRO_0000007993.
FT   CHAIN        38    225       Endo-1,4-beta-xylanase B.
FT                                /FTId=PRO_0000007994.
FT   DOMAIN       37    225       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    121    121       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    212    212       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
FT   CONFLICT     16     16       A -> V (in Ref. 2; AAM08362, 3; AAM95167,
FT                                4; ABA00146, 5; AAS46914 and 7;
FT                                ACA51680). {ECO:0000305}.
FT   CONFLICT     25     26       AQ -> VE (in Ref. 2; AAM08362, 3;
FT                                AAM95167, 4; ABA00146, 5; AAS46914 and 7;
FT                                ACA51680). {ECO:0000305}.
FT   CONFLICT     33     33       M -> K (in Ref. 2; AAM08362, 3; AAM95167,
FT                                4; ABA00146, 5; AAS46914 and 7;
FT                                ACA51680). {ECO:0000305}.
FT   CONFLICT     70     70       A -> S (in Ref. 2; AAM08362, 3; AAM95167,
FT                                4; ABA00146, 5; AAS46914 and 7;
FT                                ACA51680). {ECO:0000305}.
FT   CONFLICT     76     76       S -> P (in Ref. 8; ACJ26382).
FT                                {ECO:0000305}.
FT   CONFLICT    130    130       D -> V (in Ref. 6; ACA24724).
FT                                {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
//
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