ID   XYNA_THESA              Reviewed;        1157 AA.
AC   P36917;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 118.
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   Thermoanaerobacterium saccharolyticum.
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacterium.
OX   NCBI_TaxID=28896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 34-41.
RC   STRAIN=ATCC 49915 / DSM 7060 / B6A-RI;
RX   PubMed=8215382; DOI=10.1128/aem.59.9.3134-3137.1993;
RA   Lee Y.-E., Lowe S.E., Zeikus J.G.;
RT   "Gene cloning, sequencing, and biochemical characterization of endoxylanase
RT   from Thermoanaerobacterium saccharolyticum B6A-RI.";
RL   Appl. Environ. Microbiol. 59:3134-3137(1993).
RN   [2]
RP   ACTIVE SITE, AND MUTAGENESIS.
RX   PubMed=8376336; DOI=10.1128/jb.175.18.5890-5898.1993;
RA   Lee Y.-E., Lowe S.E., Henrissat B., Zeikus J.G.;
RT   "Characterization of the active site and thermostability regions of
RT   endoxylanase from Thermoanaerobacterium saccharolyticum B6A-RI.";
RL   J. Bacteriol. 175:5890-5898(1993).
CC   -!- FUNCTION: Endo-acting enzyme that randomly cleaves the internal
CC       xylosidic linkages of the xylan backbone, yielding xylooligosaccharides
CC       of various lengths which are further hydrolyzed to xylose molecules by
CC       beta-xylosidase (EC 3.2.1.37). Requires at least three xylose residues
CC       for catalytic activity. Does not have activity against xylobiose.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5.;
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius.;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- INDUCTION: By xylan and xylose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; M97882; AAA21812.1; ALT_SEQ; Genomic_DNA.
DR   PIR; A48490; A48490.
DR   AlphaFoldDB; P36917; -.
DR   SMR; P36917; -.
DR   CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR   CAZy; CBM9; Carbohydrate-Binding Module Family 9.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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   CDD; cd00005; CBM9_like_1; 1.
DR   Gene3D; 2.60.40.1190; -; 2.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR010502; Carb-bd_dom_fam9.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR001119; SLH_dom.
DR   PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF06452; CBM9_1; 2.
DR   Pfam; PF02018; CBM_4_9; 2.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   Pfam; PF00395; SLH; 2.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49344; CBD9-like; 2.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
DR   PROSITE; PS51272; SLH; 2.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Repeat; Signal; Xylan degradation.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000269|PubMed:8215382"
FT   CHAIN           34..1157
FT                   /note="Endo-1,4-beta-xylanase A"
FT                   /id="PRO_0000007980"
FT   DOMAIN          38..189
FT                   /note="CBM-cenC 1"
FT   DOMAIN          195..343
FT                   /note="CBM-cenC 2"
FT   DOMAIN          352..675
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   DOMAIN          1051..1114
FT                   /note="SLH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT   DOMAIN          1115..1157
FT                   /note="SLH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT   ACT_SITE        495
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        537
FT                   /evidence="ECO:0000269|PubMed:8376336"
FT   ACT_SITE        600
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061,
FT                   ECO:0000269|PubMed:8376336"
FT   MUTAGEN         537
FT                   /note="D->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:8376336"
FT   MUTAGEN         600
FT                   /note="E->Q: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:8376336"
FT   MUTAGEN         602
FT                   /note="D->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:8376336"
SQ   SEQUENCE   1157 AA;  128380 MW;  51FA6004497EC58B CRC64;
     MMKNNVDRIV SIVTALIMIF GASLFSPPIR VFADDTNINL VSNGDFESGT IDGWIKQGNP
     TLAVTTEQAI GQYSMKVTGR TQTYEGPAYS FLGKMQKGES YSVSLKVRLV SGQNSSNPLI
     TVTMFREDDN GKHYDTIVWQ KQVSEDSWTT VSGTYTLDYI GTLKTLYMYV ESPDPTLEYY
     IDDVVVTTQN PIQVGNVIAN ETFENGNTSG WIGTGSSVVK AVYGVAHSGD YSLLTTGRTA
     NWNGPSYDLT GKIVPGQQYN VDFWVKFVNG NDTEQIKATV KATSDKDNYI QVNDFANVNK
     GEWTEIKGSF TLPVADYSGI SIYVESQNPT LEFYIDDFSV IGEISNNQIT IQNDIPDLYS
     VFKDYFPIGV AVDPSRLNDA DPHAQLTAKH FNMLVAENAM KPESLQPTEG NFTFDNADKI
     VDYAIAHNMK MRGHTLLWHN QVPDWFFQDP SDPSKSASRD LLLQRLKTHI TTVLDHFKTK
     YGSQNPIIGW DVVNEVLDDN GNLRNSKWLQ IIGPDYIEKA FEYAHEADPS MKLFINDYNI
     ENNGVKTQAM YDLVKKLKSE GVPIDGIGMQ MHININSNID NIKASIEKLA SLGVEIQVTE
     LDMNMNGNIS NEALLKQARL YKQLFDLFKA EKQYITAVVF WGVSDDVTWL SKPNAPLLFD
     SKLQAKPAFW AVVDPSKAIP DIQSAKALEG SPTIGANVDS SWKLVKPLYV NTYVEGTVGA
     TATVKSMWDT KNLYLLVQVS DNTPSNNDGI EIFVDKNDDK STSYETDDER YTIKRDGTGS
     SDITKYVTSN ADGYVAQLAI PIEDISPAVN DKIGFDIRIN DDKGNGKIDA ITVWNDYTNS
     QNTNTSYFGD IVLSKSAQIA TAIYGTPVID GKVDDIWNNV EPISTNTWIL GSNGATATQK
     MMWDDKYLYV LADVTDSNLN KSSINPYEQD SVEVFVDQNN DKTTYYENDD GQYRVNYDNE
     QSFGGSTNSN GFKSATSLTQ SGYIVEEAIP WTSITPSNGT IIGFDLQVNN ADENGKRTGI
     VTWCDPSGNS WQDTSGFGNL LLTGKPSGAL KKGVTFDDIK NSWAKDAIEV LASRHIVEGM
     TDTQYEPNKT VTRAEFTAMI LRLLNIKEEQ YSGEFSDVNS GDWYANAIEA AYKAGIIEGD
     GKNARPNDSI TREEMTQ
//