ID E0RS15_SPITD Unreviewed; 371 AA.
AC E0RS15;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN OrderedLocusNames=STHERM_c08530 {ECO:0000313|EMBL:ADN01802.1};
OS Spirochaeta thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=665571 {ECO:0000313|EMBL:ADN01802.1, ECO:0000313|Proteomes:UP000001296};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 6192;
RA Angelov A., Mientus M., Wittenberg S., Lehmann R., Liesegang H., Daniel R.,
RA Liebl W.;
RT "The genome sequence of Spirochaeta thermophila DSM6192.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADN01802.1, ECO:0000313|Proteomes:UP000001296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49972 / DSM 6192 / RI 19.B1
RC {ECO:0000313|Proteomes:UP000001296};
RX PubMed=20935097; DOI=10.1128/JB.01023-10;
RA Angelov A., Liebl S., Ballschmiter M., Bomeke M., Lehmann R., Liesegang H.,
RA Daniel R., Liebl W.;
RT "Genome sequence of the polysaccharide-degrading, thermophilic anaerobe
RT Spirochaeta thermophila DSM 6192.";
RL J. Bacteriol. 192:6492-6493(2010).
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|RuleBase:RU361174}.
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DR EMBL; CP001698; ADN01802.1; -; Genomic_DNA.
DR AlphaFoldDB; E0RS15; -.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR PaxDb; 665571-STHERM_c08530; -.
DR KEGG; sta:STHERM_c08530; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_020161_6_1_12; -.
DR Proteomes; UP000001296; Chromosome.
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 Gene3D; 3.20.20.80; Glycosidases; 1.
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; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
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:ADN01802.1}.
FT DOMAIN 38..371
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 277
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 371 AA; 42207 MW; 45FE56FF8B67648A CRC64;
MMKTSTGSTH PVPRGAILIM AFLVGLGVLH PAGMKERSMA YAPLKEVYKD YFSIGAAVKL
GEYNSTPFYQ AYGEDVLQHF DSFTAENGMK PENVYRNGTY DFTYGDRLVR YAREHGAVVR
GHTLVWHNQT SSLIPRPLPK EEARRLLEEY ISTVAGHFRG GIHAWDVVNE AVGDGSQWRT
SSPWYQSYGG PEYIREAFEY ARMADPDARL FYNDYNVVQP AKRARIVRMI EELDLVEAGL
DGIGIQAHWN LQWPSAEEIS RTIETFASMG LEVHITELDI DCYNGNPAAP EMAYTSELEE
KLARRYAEIF EVLRRHKGEV TSVTFWGIAD PDSWLNGFSG GRFLEKRREN YPLLFDGKGD
PKEAFFSIIN W
//
