ID   XYN4_CALSA              Reviewed;         312 AA.
AC   P23557;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Putative endo-1,4-beta-xylanase;
DE            Short=Xylanase;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase;
DE   AltName: Full=ORF4;
OS   Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX   NCBI_TaxID=44001;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2111111; DOI=10.1128/aem.56.4.1017-1024.1990;
RA   Luethi E., Love D.R., McAnulty J., Wallace C., Caughey P.A., Saul D.J.,
RA   Bergquist P.L.;
RT   "Cloning, sequence analysis, and expression of genes encoding xylan-
RT   degrading enzymes from the thermophile 'Caldocellum saccharolyticum'.";
RL   Appl. Environ. Microbiol. 56:1017-1024(1990).
CC   -!- FUNCTION: Could be a xylanase. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; M34459; AAA23062.1; -; Genomic_DNA.
DR   PIR; D37202; D37202.
DR   AlphaFoldDB; P23557; -.
DR   SMR; P23557; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   OMA; GALTCEN; -.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
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; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Xylan degradation.
FT   CHAIN           1..312
FT                   /note="Putative endo-1,4-beta-xylanase"
FT                   /id="PRO_0000184068"
FT   DOMAIN          1..301
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        104
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        216
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|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