ID   XYNA_PRERU              Reviewed;         369 AA.
AC   P48789;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Endo-1,4-beta-xylanase A;
DE            Short=Xylanase A;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase A;
DE   Flags: Precursor;
GN   Name=xynA;
OS   Prevotella ruminicola (Bacteroides ruminicola).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Xylanibacter.
OX   NCBI_TaxID=839;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B14;
RX   PubMed=7487028; DOI=10.1128/aem.61.8.2958-2964.1995;
RA   Gasparic A., Martin J., Daniel A.S., Flint H.J.;
RT   "A xylan hydrolase gene cluster in Prevotella ruminicola B(1)4: sequence
RT   relationships, synergistic interactions, and oxygen sensitivity of a novel
RT   enzyme with exoxylanase and beta-(1,4)-xylosidase activities.";
RL   Appl. Environ. Microbiol. 61:2958-2964(1995).
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}.
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; Z49241; CAA89207.1; -; Genomic_DNA.
DR   AlphaFoldDB; P48789; -.
DR   SMR; P48789; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
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; 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; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Signal; Xylan degradation.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..369
FT                   /note="Endo-1,4-beta-xylanase A"
FT                   /id="PRO_0000007976"
FT   DOMAIN          21..367
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        156
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        261
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   369 AA;  42524 MW;  EFDBB3E9D77F92D2 CRC64;
     MRKLTQFCLG LMLLPIAAVA QNQPTMKDVL GKYFLVGTAL NSHQIWTHDP KIVHAITDNF
     NSVVAENCMK GEIIHPEEDY YDWHDADQLV KFAEQHKMTV HGHCLVWHSQ APKWMFTDKE
     GKEVTREVLI DRMYHHITNV VKRYKGKIKG WDVVNEAILD NGEYRQSPYY KIIGPDFIKL
     AFIFAHQADP DAELYYNDYS MSIPAKRNAV VKLVKELKAA GCRIDAVGMQ SHNGFNYPNL
     EDYENSIKAF IAAGVDVQFT ELDVNMLPNP KSFGGAEISQ NYKYNKELNP YVNGLTKAAQ
     KTFDQQYLSF FKIYRKYVDH IKRVTVWGVD DGSSWLNGWP VPGRTNYGLL IDRNYKVKPV
     VKEIIKLYE
//