ID   XYN1_HUMGT              Reviewed;         429 AA.
AC   P79046;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Endo-1,4-beta-xylanase 1;
DE            Short=Xylanase 1;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 1;
DE   Flags: Precursor;
GN   Name=xyn1;
OS   Humicola grisea var. thermoidea.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Trichocladium;
OC   Trichocladium griseum.
OX   NCBI_TaxID=5528;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=9339567; DOI=10.1271/bbb.61.1593;
RA   Iikura H., Takashima S., Nakamura A., Masaki H., Uozumi T.;
RT   "Cloning of a gene encoding a putative xylanase with a cellulose-binding
RT   domain from Humicola grisea.";
RL   Biosci. Biotechnol. Biochem. 61:1593-1595(1997).
CC   -!- FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a
CC       major structural heterogeneous polysaccharide found in plant biomass
CC       representing the second most abundant polysaccharide in the biosphere,
CC       after cellulose.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- INDUCTION: Induced by xylan and Avicel, and repressed by glucose.
CC       {ECO:0000269|PubMed:9339567}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; AB001030; BAA19220.1; -; Genomic_DNA.
DR   PIR; JC5861; JC5861.
DR   AlphaFoldDB; P79046; -.
DR   SMR; P79046; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030248; F:cellulose 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-UniPathway.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490; PTHR31490; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00236; fCBD; 1.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Disulfide bond; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..429
FT                   /note="Endo-1,4-beta-xylanase 1"
FT                   /id="PRO_0000429617"
FT   DOMAIN          43..336
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   DOMAIN          393..429
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          364..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..394
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        150
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        257
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        286..292
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   429 AA;  47018 MW;  9B7A6B47A25FDE57 CRC64;
     MQTKSILTAA LLAAAPASAQ LHELAVKAGL KYFGTALREG AINSDQQYNR ILSDTREFGQ
     LVPENGQKWD ATEPNRGQFN FQQGDITANK ARQNGQGLRC HTLIWYSQLP GWVSSGNWNR
     QTLEAVMKTH IDNVMGHYKG QCYAWDVVNE AVDDNGQWRN NVFLRVFGTD YLPLSFNLAK
     AADPDTKLYY NDYNLEYNQA KTDRAVELVK IVQDAGAPID GVGFQGHLIV GSTPTRQQLA
     TVLRRFTSLG VEVAYTELDI RHSRLPASQQ ALVTQGNDFA NVVGSCLDVA GCVGVTVWSF
     TDKYSWIPET FSGEGDALIY DRNFNKKPAW TSISSVLAAA ATNPPASSST SVVVPTTTFV
     TTTTTPPPIS SPIVPSTTTT SAVPTTTVSP PEPEQTRWGQ CGGIGWNGPT KCQSPWTCTR
     LNDWYFQCL