GenomeNet

Database: UniProt
Entry: D2KFL8_9FIRM
LinkDB: D2KFL8_9FIRM
Original site: D2KFL8_9FIRM 
ID   D2KFL8_9FIRM            Unreviewed;       173 AA.
AC   D2KFL8;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   08-NOV-2023, entry version 32.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
DE   Flags: Fragment;
OS   Cellulosilyticum ruminicola.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC   Cellulosilyticum.
OX   NCBI_TaxID=425254 {ECO:0000313|EMBL:ACZ98620.1};
RN   [1] {ECO:0000313|EMBL:ACZ98620.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.5065 {ECO:0000313|EMBL:ACZ98620.1};
RX   PubMed=20400560; DOI=10.1128/AEM.03124-09;
RA   Cai S., Li J., Hu F.Z., Zhang K., Luo Y., Janto B., Boissy R., Ehrlich G.,
RA   Dong X.;
RT   "Cellulosilyticum ruminicola, a newly described rumen bacterium that
RT   possesses redundant fibrolytic-protein-encoding genes and degrades
RT   lignocellulose with multiple carbohydrate- borne fibrolytic enzymes.";
RL   Appl. Environ. Microbiol. 76:3818-3824(2010).
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; GU211296; ACZ98620.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2KFL8; -.
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; IPR001000; GH10_dom.
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; (Trans)glycosidases; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {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|RuleBase:RU361174};
KW   Xylan degradation {ECO:0000313|EMBL:ACZ98620.1}.
FT   DOMAIN          1..173
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   REGION          122..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         173
FT                   /evidence="ECO:0000313|EMBL:ACZ98620.1"
SQ   SEQUENCE   173 AA;  19474 MW;  542534E9F3AD8E53 CRC64;
     MKPEAMLDYD ATIKYMEENN GDETHPQVHL SPEAIATLDF ARDKGIPIRG HVLVWHSQTP
     NWLFTKGYSK AADAEFVSKD VMLQRLENYI DAVFKILDEQ YPDVKFYAFD VVNEAVNPSS
     PDGLRFPAKS ATTSGDDGNN ENANNSMWMT TIGAEHIEKA FEYARAASKK YTS
//
DBGET integrated database retrieval system