ID A0A1G7L8F1_9PSEU Unreviewed; 446 AA.
AC A0A1G7L8F1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=SAMN05216553_101708 {ECO:0000313|EMBL:SDF45299.1};
OS Lentzea fradiae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=200378 {ECO:0000313|EMBL:SDF45299.1, ECO:0000313|Proteomes:UP000199623};
RN [1] {ECO:0000313|Proteomes:UP000199623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3506 {ECO:0000313|Proteomes:UP000199623};
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|RuleBase:RU361174}.
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DR EMBL; FNCC01000001; SDF45299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7L8F1; -.
DR STRING; 200378.SAMN05216553_101708; -.
DR OrthoDB; 9815836at2; -.
DR Proteomes; UP000199623; 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; 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; 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; PF00553; CBM_2; 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 PROSITE; PS51173; CBM2; 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}; Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:SDF45299.1}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..446
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011643591"
FT DOMAIN 32..330
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 347..446
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 446 AA; 46796 MW; AEBE7B614BA1E21D CRC64;
MKLTSRSVSL VPIMATALAA ALGAVLVVSA PANAATTLGA AAAQSGRYFG TAVAAGRLSD
QTYVNILNTE FNMVTAENEM KWDATEPNRG QFNYSGGDRI LNQAVGNGSR VRGHALLWHQ
QEPGWARSME GSSLRQAMIN HVTQVATHYR GKIYAWDVVN EAFADGGSGG RRDSNLQRTG
NDWIEAAFRA ARAADPAAKL CYNDYNTDGI NPKSTGIYNM VRDFKARGVP IDCVGFQSHL
TNNAPSDYRA NLQRFADLGV EVQITELDIA GSNQANAYRD VTNACMAIRA CTGITVWGIR
DTDSWRTGEN PLLFTGSGAK KPAYNAVLDA LNAGGPGPTT TTTTTSNNPG PGGCTASVSL
NQWNDGFVAS VKVTAGSSAL RGWRVTATLS NGTVTSSWSS NRSGNSGAVT FTNVDYNGSV
PAGGSTEFGF QGTGSGAGLN PSCTAT
//
