ID H2JDB7_9CLOT Unreviewed; 541 AA.
AC H2JDB7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=Clo1100_0910 {ECO:0000313|EMBL:AEY65167.1};
OS Clostridium sp. BNL1100.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=755731 {ECO:0000313|EMBL:AEY65167.1, ECO:0000313|Proteomes:UP000007324};
RN [1] {ECO:0000313|EMBL:AEY65167.1, ECO:0000313|Proteomes:UP000007324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BNL1100 {ECO:0000313|EMBL:AEY65167.1,
RC ECO:0000313|Proteomes:UP000007324};
RX PubMed=23209234; DOI=10.1128/JB.01908-12;
RA Li L.L., Taghavi S., Izquierdo J.A., van der Lelie D.;
RT "Complete Genome Sequence of Clostridium sp. Strain BNL1100, a Cellulolytic
RT Mesophile Isolated from Corn Stover.";
RL J. Bacteriol. 194:6982-6983(2012).
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; CP003259; AEY65167.1; -; Genomic_DNA.
DR RefSeq; WP_014312550.1; NC_016791.1.
DR AlphaFoldDB; H2JDB7; -.
DR STRING; 755731.Clo1100_0910; -.
DR KEGG; clb:Clo1100_0910; -.
DR PATRIC; fig|755731.4.peg.900; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_438535_0_0_9; -.
DR OrthoDB; 9809277at2; -.
DR Proteomes; UP000007324; 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; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd14256; Dockerin_I; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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:SF1; ENDO-1,4-BETA-XYLANASE 1; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00606; CBD_IV; 1.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS51175; CBM6; 1.
DR PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 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}; Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:AEY65167.1}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..541
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038631209"
FT DOMAIN 52..327
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 345..468
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 473..539
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
FT ACT_SITE 262
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 541 AA; 59675 MW; 9ACD2A7FA497C1C6 CRC64;
MINKSKNRKF RIFSILFSAL LCTCIINSSL PLTADAAMAT GKAKFVGNIW YDGNPPSKFG
DYWNQITPEN ATKWGSCESQ QGVYNFSQAK AMYNYCKTNK IPFKFHTLIW GSQYPNWLGN
LSGSARKTAI ENWYKAAAQN FPDAEYIDVV NEAMPGHAPF PYKNDIGGDN GLYGTGWDWI
VWSFEMARKY FPNSKLLIND YNVLNEWSCL DQYIPVVKIL KARNLIDGVG CQSHSLENTS
AANLKSRLDK LAATGVPIYI SELDLNIADD NTQKNKMQEL FPVMYEHSAV KGITIWGYLQ
GHTWISNSHL IRSDGSERPA MTWLKQYMAS VPGDNTPVEP RSAFTKLEAE SYNDQSGIQN
VTCDEGTEAV GYTENGDYTV YKSIDFGSGA TSFQVRVSSA TSGGNIEIRL DSATGTLVGT
CPVAGTSGWQ VFTDAKCSVS GVSGKHDLYL KFTGGSGYLF NLNWFMFGNT PASTDKIGDL
NSDGQIDALD FQVLKKCILG TGTVENTKLA DLDASGTIDA LDFVLMKQYL LGQITIFPAD
K
//
