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
//
