GenomeNet

Database: UniProt
Entry: A0A1H0IUL0_9PSEU
LinkDB: A0A1H0IUL0_9PSEU
Original site: A0A1H0IUL0_9PSEU 
ID   A0A1H0IUL0_9PSEU        Unreviewed;       457 AA.
AC   A0A1H0IUL0;
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=SAMN05421507_102237 {ECO:0000313|EMBL:SDO34731.1};
OS   Lentzea jiangxiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Lentzea.
OX   NCBI_TaxID=641025 {ECO:0000313|EMBL:SDO34731.1, ECO:0000313|Proteomes:UP000199691};
RN   [1] {ECO:0000313|EMBL:SDO34731.1, ECO:0000313|Proteomes:UP000199691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.6609 {ECO:0000313|EMBL:SDO34731.1,
RC   ECO:0000313|Proteomes:UP000199691};
RA   de Groot N.N.;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FNIX01000002; SDO34731.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0IUL0; -.
DR   STRING; 641025.SAMN05421507_102237; -.
DR   OrthoDB; 9815836at2; -.
DR   Proteomes; UP000199691; 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:SDO34731.1}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..457
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011764784"
FT   DOMAIN          32..335
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   DOMAIN          358..457
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          340..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          438..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        269
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   457 AA;  48538 MW;  ACEDF3407D9B0EF7 CRC64;
     MRLTSKSVTL IPIIATVATA AIGATLIAPP VANAATTLAA AAQQSGRYFG TAVAANRLSD
     STYVGILNRE FDMVTAENEM KMDATEPAQN RFNYGNADRI VNHARGQGKR IRGHALAWHS
     QQPAWMQSMS GTTLRNAMLN HVTQVATYYR GKIYAWDVVN EAFADGSSGA RRDSNLQRTG
     NDWIEAAFRA ARAADPGAKL CYNDYNTDDW THAKTQAVYR MVQDFKSRGV PIDCVGLQSH
     FNNNSPVPSN YQTTLQNFAN LGVDVQITEL DIEGSGSTQA QNYQRVTQAC LNVARCTGIT
     VWGIRDTDSW RASGTPLLFD GNGNKKAAYN STLAALNAAG GPGPTTTTTT TTTTTTSNDP
     GNGACTATVS LNQWNEGFVA TVKVTAGSSA LRGWTVTTTL SDGTVTGSWS ANRSGNSGSV
     TWTNVDYNAE VPAGGSTEFG FQGSGSGAEL NPTCSAR
//
DBGET integrated database retrieval system