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XYNB_THENE
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   25-MAY-2022, entry version 74.
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:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; Z49961; CAA90235.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q60041; -.
DR   SMR; Q60041; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
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; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490; PTHR31490; 1.
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
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..346
FT                   /note="Endo-1,4-beta-xylanase B"
FT                   /id="PRO_0000007988"
FT   DOMAIN          41..338
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        153
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        259
FT                   /note="Nucleophile"
FT                   /evidence="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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