GenomeNet

Database: UniProt
Entry: W0FM23_9BACT
LinkDB: W0FM23_9BACT
Original site: W0FM23_9BACT 
ID   W0FM23_9BACT            Unreviewed;       372 AA.
AC   W0FM23;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
OS   uncultured bacterium Contig28b.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=1393549 {ECO:0000313|EMBL:AHF24514.1};
RN   [1] {ECO:0000313|EMBL:AHF24514.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24223817;
RA   Wang L., Hatem A., Catalyurek U.V., Morrison M., Yu Z.;
RT   "Metagenomic insights into the carbohydrate-active enzymes carried by the
RT   microorganisms adhering to solid digesta in the rumen of cows.";
RL   PLoS ONE 8:E78507-E78507(2013).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000256|RuleBase:RU361174}.
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; KC246796; AHF24514.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0FM23; -.
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; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490:SF88; 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; PS00591; GH10_1; 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|ARBA:ARBA00023295, 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};
KW   Xylan degradation {ECO:0000313|EMBL:AHF24514.1}.
FT   DOMAIN          35..369
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   ACT_SITE        296
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   372 AA;  42141 MW;  9D1C076DF48EC689 CRC64;
     MIRRVASILL AMLFLLVYAG CTGEEEMQDL LSTETERLPS LREIYEAHFD FGAAAPQRVF
     SDPKWRNLML QQFSILTPEN ELKPDSVLDI SASRELVKET GDESQAAVHF DAAKPLLTFA
     RNNGMKVHGH VLVWHSQTPE AFFHEGYDSA RPMVSREIML GRMEHYIRGV MEYMQTNYPG
     MIVSWDVLNE AIDDGTNGLR KSLWFQVIGE DYPEYAFTFA RKYAPEGTLL YYNDYNTAYS
     GKRVGIIKLL KRLIADGNID GYGFQMHHSV NTPSMYEIKA AVDAIAALGL RLRVSELDIG
     VDSDKDASFE MQAEKYAAIM KLLMSRSDQV EAVQVWGLTD AMSWRSKDKP LLFDAEGNPK
     PAFWAVADPT KY
//
DBGET integrated database retrieval system