ID   XYNA_BUTFI              Reviewed;         411 AA.
AC   P23551;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-MAY-2023, entry version 91.
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   Butyrivibrio fibrisolvens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=49;
RX   PubMed=2198249; DOI=10.1128/jb.172.8.4247-4254.1990;
RA   Mannarelli B.M., Evans S., Lee D.;
RT   "Cloning, sequencing, and expression of a xylanase gene from the anaerobic
RT   ruminal bacterium Butyrivibrio fibrisolvens.";
RL   J. Bacteriol. 172:4247-4254(1990).
CC   -!- FUNCTION: B.fibrisolvens is located in the rumen of ruminant animals,
CC       where it contributes to the animal's digestion of plant material by
CC       hydrolyzing hemicellulose with its xylanases.
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   PIR; A37755; A37755.
DR   AlphaFoldDB; P23551; -.
DR   SMR; P23551; -.
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..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..411
FT                   /note="Endo-1,4-beta-xylanase A"
FT                   /id="PRO_0000007970"
FT   DOMAIN          34..382
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   REGION          387..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..411
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        201
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        311
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   411 AA;  46659 MW;  4EA4AC50D8979DD5 CRC64;
     MKKFKIRKLM ARVLALALVF STFFMVSKVD ANAASYNLME TYGAKYGYSG NCVHTHMLRD
     SRIVNAIKKD SNIVTLGNEM KPDYLLGSRQ ATLISVDEAK RLGYYIPSNY KERYVPKIDF
     RTVDEAVKIC YENGLKMRGH TLVWHSQTPT WLFRENYSGN GRFVNTATMD ARLEFYVKSV
     MGHFYSGKYG STLVYWDVCN ETLHAQNSGW EAVYGSNKTN AVYVKKAFNY AYQVLEQYKL
     TNSVKLFYND YNTYMEVNDV IKLVNYINQG KKVCAGVGMQ SHLGTGFPSV DYYTNALNSF
     LRAGFEVQIT ELDITNKGDY DLNNYAYRLF KNINAAKKNG GNISCITWWG PSDAETWIRN
     EKPLIWSNIG VAKPAYDEVV KAFTETFGNP GSFTPQPTIT PQPTPTPSGQ T
//