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Database: UniProt
Entry: B6DQK8_PHAND
LinkDB: B6DQK8_PHAND
Original site: B6DQK8_PHAND 
ID   B6DQK8_PHAND            Unreviewed;       356 AA.
AC   B6DQK8;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
OS   Phaeosphaeria nodorum (Glume blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=13684 {ECO:0000313|EMBL:ACI04505.1};
RN   [1] {ECO:0000313|EMBL:ACI04505.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S-81-B13B {ECO:0000313|EMBL:ACI04505.1};
RA   Malkus A., Chiu E.Y., Ueng P.P.;
RT   "Genetic mapping of Phaeosphaeria nodorum.";
RL   Submitted (AUG-2008) 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; Evidence={ECO:0000256|RuleBase:RU361174};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|ARBA:ARBA00004851}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000256|ARBA:ARBA00007495, ECO:0000256|RuleBase:RU361174}.
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DR   EMBL; FJ151545; ACI04505.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6DQK8; -.
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   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490:SF35; ENDO-1,4-BETA-XYLANASE; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361174};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361174}; Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:ACI04505.1}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..356
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002841822"
FT   DOMAIN          33..347
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
SQ   SEQUENCE   356 AA;  38801 MW;  856459703EC3E5E7 CRC64;
     MLFTSFTTAL ALASSAAAIP TFGLEPRQAA TLNAAIVARG RSYIGTSLTI RSDTQESNII
     KSEFGSITPE NSMKWDATEP NRGQFTFNGA DQVANFATQN NKQMRCHTLV WYSQLPSWVN
     QINNNATLMS VMENHINTVM GRYKGKCTHW DVVNEALNED GTNRDNVFLR VIGEQYMPIA
     FRMAAAADPA AKLYYNDYNL EYGGAKHTGA LRIVKLVQSW GVKIDGVGLQ AHLTSESTGT
     QNTPTPSVAV LTKTLQDYAD LGVDVAYTEL DIRSNTPSNS GKETIAAAAW ARVAQSCINV
     SRCVGITIWG VKDGYSWVPG TFPGEGSALL WNDSYQKKPA YTAFLNVLNG QNVTLA
//
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