ID B9K945_THENN Unreviewed; 1022 AA.
AC B9K945;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN OrderedLocusNames=CTN_1302 {ECO:0000313|EMBL:ACM23478.1};
OS Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Thermotoga.
OX NCBI_TaxID=309803 {ECO:0000313|EMBL:ACM23478.1, ECO:0000313|Proteomes:UP000000445};
RN [1] {ECO:0000313|Proteomes:UP000000445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E
RC {ECO:0000313|Proteomes:UP000000445};
RA Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J.,
RA Kim J.J., Park K.J., Lee S.Y.;
RT "The genome sequence of the hyperthermophilic bacterium Thermotoga
RT neapolitana.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACM23478.1, ECO:0000313|Proteomes:UP000000445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E
RC {ECO:0000313|Proteomes:UP000000445};
RX PubMed=19129632; DOI=10.1271/bbb.80567;
RA Lee D., Seo H., Park C., Park K.;
RT "WeGAS: a web-based microbial genome annotation system.";
RL Biosci. Biotechnol. Biochem. 73:213-216(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000256|RuleBase:RU361174};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000256|ARBA:ARBA00007495, ECO:0000256|RuleBase:RU361174}.
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DR EMBL; CP000916; ACM23478.1; -; Genomic_DNA.
DR RefSeq; WP_015919776.1; NC_011978.1.
DR AlphaFoldDB; B9K945; -.
DR STRING; 309803.CTN_1302; -.
DR CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR CAZy; CBM9; Carbohydrate-Binding Module Family 9.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR KEGG; tna:CTN_1302; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_001408_1_0_0; -.
DR Proteomes; UP000000445; Chromosome.
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 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361174};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361174};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361174};
KW Xylan degradation {ECO:0000313|EMBL:ACM23478.1}.
FT DOMAIN 327..655
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 571
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 1022 AA; 116783 MW; E42AFD3D3D28AFA4 CRC64;
MRSLLRLCLF LVLVSALVTG GEIMNFEREE EGVSPFGRAV VTLSQDVSFR GVYSLKVDGR
TSLWDGVEFD LTGKVSPGKE YRVFFYVYQT SNTPQLFSVL SRVVDESGER YEILLDKVVT
PDVWKKMELI FTSPQRAEKF SLIVASPERT NFPFYIDELQ LSSPDEVQEP PPVLHCSFES
ETAEGWIPRG NAKLQVTSRV SHTGRNALFI SERSASWEGT QFDLKSIVKP GKTYTFEMWV
YQDSGSPVGI LMRMTRKFEN EITTKHPIWL YGRTVPSGKW VKLFGIFGLP EGIDVDQLVL
YVYTDGSNTD FYVDDVKIYD KPLVSFEEDV PSLKEIFKDQ FKIGAGISEK SILTPFDLEF
LKKHFNSVTE RNNMKPVNLL AGVENGRLKF DFSLADLFVD TALKNGISVR GHTLVWHNQT
PEWFFKDENG NLLSKEEMTE RLREYIHTVV GHFKGKVYAW DVVNEAVDPN QPDGLRRSTW
YQIMGPDYIE LAFRFAREAD PNAKLFYNDY NTFEPKKRDI IYNLVKSLKE KGLIDGIGMQ
CHISLATDIR QIEEAIKKFS TIPGIEIHIT ELDISVYRDS TSNYSEAPRT ALIEQAHKMA
QLFKIFKKYS NVITNVTFWG LKDDYSWRAT RRNDWPLIFD KDYQAKLAYW AIVAPEVLPP
LPKESKISEG EAVVVGMMDD SYMMSKPIEI YDEEGNVKAT IRAIWKDSTI YVYGEVQDAT
KKPAEDGVAI FINPNNERTP YLQPDDTYVV LWTNWKSEVN REDVEVKKFV GPGFRRYSFE
MSITIPGVEF KKDSYIGFDV AVIDDGKWYS WSDTTNSQKT NTMNYGTLKL EGVMVATAKY
GTPVIDGEID DIWNTTEEIE TKSVAMGSLE KNATAKVRVL WDEENLYVLA IVKDPVLNKD
NSNPWEQDSV EIFIDENNHK TGYYEDDDAQ FRVNYMNEQS FGTGASAARF KTAVKLIEGG
YIVEAAIKWK TIKPSPNTVI GFNVQVNDAN EKGQRVGIIS WSDPTNNSWR DPSKFGNLKL
LK
//
