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Database: UniProt
Entry: Q60041
LinkDB: Q60041
Original site: Q60041 
ID   XYNB_THENE              Reviewed;         346 AA.
AC   Q60041;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   05-JUL-2017, entry version 68.
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   Thermotoga neapolitana.
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=2337;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Z2706-MC24;
RA   Zverlov V., Piotukh K., Velikodvorskaja G., Goetz F., Borriss R.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-xylosidic
CC       linkages in xylans.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F)
CC       family. {ECO:0000305}.
DR   EMBL; Z49961; CAA90235.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q60041; -.
DR   SMR; Q60041; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   eggNOG; ENOG4105D9F; Bacteria.
DR   eggNOG; COG3693; LUCA.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001000; GH10.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Signal; Xylan degradation.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    346       Endo-1,4-beta-xylanase B.
FT                                /FTId=PRO_0000007988.
FT   DOMAIN       41    338       GH10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01096}.
FT   ACT_SITE    153    153       Proton donor. {ECO:0000250}.
FT   ACT_SITE    259    259       Nucleophile. {ECO:0000250}.
SQ   SEQUENCE   346 AA;  40338 MW;  5E96C39D46173595 CRC64;
     MKGLPALLLL LIGCVSSFGS QDVPLRVLAE KLNIHIGFAA GNNFWSLPDA EKYMEVAKRE
     FNILTPGNQM KWDTIHPERN RYNFEPAEKH VEFALKNDMI VHGHTLVWHN QLPGWLTGQE
     WSKEELLNIL EDHVKTVVSH FRGRVKIWDV VNEAVSDSGT YRESIWYRTI GPEYIEKALI
     WAKEADPDAI LIYNDYNIEE INAKSNFVYN MIKNLREKGV PIDGIGFQMH IDYRGINYES
     FKKNLERFAE LGLQIYITEM DRGFPLGGSV GYYLKKQAEV YRRIFEICLD NPAVRAIQFW
     GFTDKYSWVP GFFKGYGKAL IFDENYNPKP CYFAIRELME EKLKER
//
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