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
//
