ID A0A1I3XNK1_9CELL Unreviewed; 706 AA.
AC A0A1I3XNK1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=SAMN05216467_2530 {ECO:0000313|EMBL:SFK21110.1};
OS Cellulomonas sp. KH9.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1855324 {ECO:0000313|EMBL:SFK21110.1, ECO:0000313|Proteomes:UP000199404};
RN [1] {ECO:0000313|Proteomes:UP000199404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH9 {ECO:0000313|Proteomes:UP000199404};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOSE01000003; SFK21110.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3XNK1; -.
DR STRING; 1855324.SAMN05216467_2530; -.
DR OrthoDB; 9815836at2; -.
DR Proteomes; UP000199404; Unassembled WGS sequence.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018366; CBM2_CS.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR044846; GH10.
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; PF00553; CBM_2; 1.
DR Pfam; PF02018; CBM_4_9; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 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 Reference proteome {ECO:0000313|Proteomes:UP000199404};
KW Xylan degradation {ECO:0000313|EMBL:SFK21110.1}.
FT DOMAIN 193..527
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 597..706
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 552..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..593
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 706 AA; 75024 MW; 6E48E66FD6947BC0 CRC64;
MPSARPVPSA LRPLVAAAAA LVAVALVAAG SLASLATPAR ALSPGVVLTS DFESGLDGWQ
ARGAASVSTT ATGARGTGSL LVQDRVDPWD GALIPVTDVF EPGTTYTIGL WLRLPDGAGT
ADLRVSVQRD LDGQPSYETV TTVEGVSSQW RQVTATYTPG LFDTASLYVE SVSSPADVMV
DDVLVSGVRY TPDLSLTPVA DAVSVPFGIA VEPQDLLGGR GDLLAHHAEQ ITPGNQMKPD
AIQPTEGTFT FAAADGLVDW ALEHDMRVYG HTLLWHQQTP AWFFQRDGAA LTTSSADQAL
LRERLRTHIE AVADHYRETY GEYGTPGNPV FAFDVVNEVI DENQPDGLRR SEWYRVLGPS
YIADAFRYAR DAFGPEVQLF INDYNSEYPD KRAPYLRLVT DLLAQGVPVD GVGHQLHVEV
GRSVPMIEDT IEAFEALDVT QAVTELDVST YRHEGEQWTT PPADRLLEQG YYYRDVLDML
ERHASSLESI TVWGLEDSRT WLRSGAAPLL FDGALQAKPA YWGIVDPSRI GTTPTPTVTQ
TPGVTPTVTS TPGVTPTVTP TPGVTPTVTP TPGVTPTVTP TPGVTPTPGV TPTVTPTPGV
TRGCRVVYTT NDWNTGFTAG VRVTNTGTSA LSGWALTFSL DGGQRVTQGW SASWTQSGAR
VTATNAAWNG SLAPGGSVEI GFNGSHPGSN PRPTSFALDG VPCAVA
//
