ID   XYNA_THENE              Reviewed;        1055 AA.
AC   Q60042;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 109.
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   AltName: Full=Endoxylanase;
DE   Flags: Precursor;
GN   Name=xynA;
OS   Thermotoga neapolitana.
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Thermotoga.
OX   NCBI_TaxID=2337;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Z2706-MC24;
RX   PubMed=8920196; DOI=10.1007/s002530050678;
RA   Zverlov V., Piotukh K., Dakhova O., Velikodvorskaya G., Borriss R.;
RT   "The multidomain xylanase A of the hyperthermophilic bacterium Thermotoga
RT   neapolitana is extremely thermoresistant.";
RL   Appl. Microbiol. Biotechnol. 45:245-247(1996).
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 5.5-6.;
CC       Temperature dependence:
CC         Optimum temperature is 102 degrees Celsius. Thermostable.;
CC   -!- DOMAIN: The C-terminal CBM-CenC domains mediate the binding of XynA to
CC       microcrystalline cellulose. CBM-CenC 2 alone can also promote cellulose
CC       binding (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; Z46945; CAA87069.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q60042; -.
DR   SMR; Q60042; -.
DR   CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR   CAZy; CBM9; Carbohydrate-Binding Module Family 9.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
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-KW.
DR   CDD; cd00005; CBM9_like_1; 1.
DR   CDD; cd00241; DOMON_like; 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; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR006311; TAT_signal.
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   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; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Repeat; Signal; Xylan degradation.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..1055
FT                   /note="Endo-1,4-beta-xylanase A"
FT                   /id="PRO_0000007987"
FT   DOMAIN          360..688
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   DOMAIN          720..851
FT                   /note="CBM-cenC 1"
FT   DOMAIN          895..1040
FT                   /note="CBM-cenC 2"
FT   REGION          30..357
FT                   /note="A"
FT   ACT_SITE        498
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        604
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   1055 AA;  119323 MW;  F939845878B87468 CRC64;
     MRKKRRGFLN ASTAVLVGIL AGFLGVVLAA TGALGFAVRE SLLLKQFLFL SFEGNTDGAS
     PFGKDVVVTA SQDVAADGEY SLKVENRTSV WDGVEIDLTG KVNTGTDYLL SFHVYQTSDS
     PQLFSVLART EDEKGERYKI LADKVVVPNY WKEILVPFSP TFEGTPAKFS LIITSPKKTD
     FVFYVDNVQV LTPKEAGPKV VYETSFEKGI GDWQPRGSDV KISISPKVAH SGKKSLFVSN
     RQKGWHGAQI SLKGILKTGK TYAFEAWVYQ ESGQDQTIIM TMQRKYSSDS STKYEWIKAA
     TVPSGQWVQL SGTYTIPAGV TVEDLTLYFE SQNPTLEFYV DDVKVVDTTS AEIKLEMNPE
     EEIPALKDVL KDYFRVGVAL PSKVFINQKD IALISKHSNS STAENEMKPD SLLAGIENGK
     LKFRFETADK YIEFAQQNGM VVRGHTLVWH NQTPEWFFKD ENGNLLSKEE MTERLREYIH
     TVVGHFKGKV YAWDVVNEAV DPNQPDGLRR STWYQIMGPD YIELAFKFAR EADPNAKLFY
     NDYNTFEPKK RDIIYNLVKS LKEKGLIDGI GMQCHISLAT DIRQIEEAIK KFSTIPGIEI
     HITELDISVY RDSTSNYSEA PRTALIEQAH KMAQLFKIFK KYSNVITNVT FWGLKDDYSW
     RATRRNDWPL IFDKDYQAKL AYWAIVAPEV LPPLPKESKI SEGEAVVVGM MDDSYMMSKP
     IEIYDEEGNV KATIRAIWKD STIYVYGEVQ DATKKPAEDG VAIFINPNNE RTPYLQPDDT
     YVVLWTNWKS EVNREDVEVK KFVGPGFRRY SFEMSITIPG VEFKKDSYIG FDVAVIDDGK
     WYSWSDTTNS QKTNTMNYGT LKLEGVMVAT AKYGTPVIDG EIDDIWNTTE EIETKSVAMG
     SLEKNATAKV RVLWDEENLY VLAIVKDPVL NKDNSNPWEQ DSVEIFIDEN NHKTGYYEDD
     DAQFRVNYMN EQSFGTGASA ARFKTAVKLI EGGYIVEAAI KWKTIKPSPN TVIGFNVQVN
     DANEKGQRVG IISWSDPTNN SWRDPSKFGN LRLIK
//