ID   A4XM47_CALS8            Unreviewed;       312 AA.
AC   A4XM47;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   02-SEP-2026, entry version 85.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   OrderedLocusNames=Csac_2405 {ECO:0000313|EMBL:ABP67982.1};
OS   Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T
OS   6331).
OC   Bacteria; Bacillati; Bacillota; Bacillota incertae sedis;
OC   Caldicellulosiruptorales; Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX   NCBI_TaxID=351627 {ECO:0000313|EMBL:ABP67982.1, ECO:0000313|Proteomes:UP000000256};
RN   [1] {ECO:0000313|EMBL:ABP67982.1, ECO:0000313|Proteomes:UP000000256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331
RC   {ECO:0000313|Proteomes:UP000000256};
RX   PubMed=18776029; DOI=10.1128/AEM.00968-08;
RA   van de Werken H.J., Verhaart M.R., VanFossen A.L., Willquist K.,
RA   Lewis D.L., Nichols J.D., Goorissen H.P., Mongodin E.F., Nelson K.E.,
RA   van Niel E.W., Stams A.J., Ward D.E., de Vos W.M., van der Oost J.,
RA   Kelly R.M., Kengen S.W.;
RT   "Hydrogenomics of the extremely thermophilic bacterium Caldicellulosiruptor
RT   saccharolyticus.";
RL   Appl. Environ. Microbiol. 74:6720-6729(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8; Evidence={ECO:0000256|PROSITE-ProRule:PRU01096,
CC         ECO:0000256|RuleBase:RU361174};
CC   -!- PATHWAY: Glycan degradation; xylan degradation. {ECO:0000256|PROSITE-
CC       ProRule:PRU01096}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01096, ECO:0000256|RuleBase:RU361174}.
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DR   EMBL; CP000679; ABP67982.1; -; Genomic_DNA.
DR   RefSeq; WP_011917904.1; NC_009437.1.
DR   AlphaFoldDB; A4XM47; -.
DR   SMR; A4XM47; -.
DR   STRING; 351627.Csac_2405; -.
DR   KEGG; csc:Csac_2405; -.
DR   eggNOG; COG3693; Bacteria.
DR   HOGENOM; CLU_020161_6_1_9; -.
DR   OrthoDB; 9809277at2; -.
DR   Proteomes; UP000000256; Chromosome.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; GH_hydrolase_sf.
DR   PANTHER; PTHR31490:SF90; ENDO-1,4-BETA-XYLANASE A; 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|PROSITE-ProRule:PRU01096};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU01096};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01096};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|PROSITE-ProRule:PRU01096};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000256};
KW   Xylan degradation {ECO:0000256|PROSITE-ProRule:PRU01096}.
FT   DOMAIN          1..301
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   ACT_SITE        104
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        216
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   312 AA;  36494 MW;  6C2A049212F9CB6E CRC64;
     MKQQYLLDYE ATKASKNGMP VCKFDSCIPA LQFCKENGIK MRGHVLVWHN QTPEWFFHKD
     YDVSKPLVDA ATMERRLESY IKQVIEFCQK NYPGVVYCWD VVNEAILDDG SWREINNNWY
     TIMKEKYVEK AFYYARKYAK KDVALFYNDY NVFLPAKREA IYNLAQKLKE KGLIDGLGLQ
     PTVGLNYPEL DSDDIDSFKT TLETFAKLGL QIHITELNFE IKGDESNRTP ENLKKQADRY
     YEMMKLLLKE DTDNGGPCNI TCVTVFGICD DYPLYKNFKQ CMYLWDKNCN PKPCFYSFLQ
     AGLDWKASLL SK
//