ID   XYNA_RUMFL              Reviewed;         954 AA.
AC   P29126;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Bifunctional endo-1,4-beta-xylanase XylA;
DE            EC=3.2.1.8;
DE   Flags: Precursor;
GN   Name=xynA;
OS   Ruminococcus flavefaciens.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=17;
RX   PubMed=1584021; DOI=10.1111/j.1365-2958.1992.tb02167.x;
RA   Zhang J.-X., Flint H.J.;
RT   "A bifunctional xylanase encoded by the xynA gene of the rumen cellulolytic
RT   bacterium Ruminococcus flavefaciens 17 comprises two dissimilar domains
RT   linked by an asparagine/glutamine-rich sequence.";
RL   Mol. Microbiol. 6:1013-1023(1992).
CC   -!- FUNCTION: Xylanase domain releases more xylo-oligosaccharides and GH10
CC       domain more xylose.
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: In the N-terminal section; belongs to the glycosyl
CC       hydrolase 11 (cellulase G) family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC       hydrolase 10 (cellulase F) family. {ECO:0000305}.
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DR   EMBL; Z11127; CAA77476.1; -; Genomic_DNA.
DR   PIR; S20907; S20907.
DR   AlphaFoldDB; P29126; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11A_RUMFL; -.
DR   PRIDE; P29126; -.
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   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033119; GH11_AS_2.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Multifunctional enzyme;
KW   Polysaccharide degradation; Repeat; Signal; Xylan degradation.
FT   SIGNAL          1..27
FT                   /note="Or 28, or 29"
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..954
FT                   /note="Bifunctional endo-1,4-beta-xylanase XylA"
FT                   /id="PRO_0000008015"
FT   DOMAIN          29..236
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   DOMAIN          624..952
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   REGION          233..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        122
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        223
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT   ACT_SITE        774
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT   ACT_SITE        884
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   954 AA;  111362 MW;  1033567D4B526EBD CRC64;
     MKLSKIKKVL SGTVSALMIA SAAPVVASAA DQQTRGNVGG YDYEMWNQNG QGQASMNPGA
     GSFTCSWSNI ENFLARMGKN YDSQKKNYKA FGNIVLTYDV EYTPRGNSYM CVYGWTRNPL
     MEYYIVEGWG DWRPPGNDGE VKGTVSANGN TYDIRKTMRY NQPSLDGTAT FPQYWSVRQT
     SGSANNQTNY MKGTIDVTKH FDAWSAAGLD MSGTLYEVSL NIEGYRSNGS ANVKSVSVTQ
     GGSSDNGGQQ QNNDWNQQNN NQQQNNDWNN WGQQNNDWNQ WNNQGQQNND WNNWGQQNND
     WNQWNNQGQQ QNNDWNNWGQ QNNDWNQWNN QGQQQNNDWN NWGQQNNDWN QWNNQGQQQN
     NDWNNWGQQN NDWNQWNNQN NNQQNAWNGW DNNNNWNQNN QQQNNWDWNN QNNWNNNQQQ
     NNDWNQWNNQ NNWNNNQQQN NDWNQWNNQG QQNNDWNQWN NQNNWNQNNN QQNAWNGWDN
     NNNWNQWDQN NQWNNQQQNN TWDWNNQNNW NNNQQNNDWN QWNNQGQQQN NDWNQWNNQN
     NNQNNGWDWN NQNNWNQNNN QQNAWNGWDN NNNWNQWGGQ NNDWNNQQQN NDWNQWNNQG
     QQQNNDWNNQ NNWNQGQQNN NNSAGSSDSL KGAFSKYFKI GTSVSPHELN SGADFLKKHY
     NSITPENELK PESILDQGAC QQKGNNVNTQ ISLSRAAQTL KFCEQNGIAL RGHTFVWYSQ
     TPDWFFRENF SQNGAYVSKD IMNQRLESMI KNTFAALKSQ YPNLDVYSYD VCNELFLNNG
     GGMRGADNSN WVKIYGDDSF VINAFKYARQ YAPAGCKLYL NDYNEYIPAK TNDIYNMAMK
     LKQLGYIDGI GMQSHLATNY PDANTYETAL KKFLSTGLEV QITELDITCT NSAEQADLYE
     KIFKLAMQNS AQIPAVTIWG TQDTVSWRSS QNPLLFSAGY QPKPAYDRVM ALAK