ID   XYNA_NAGAL              Reviewed;         332 AA.
AC   P07529;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Endo-1,4-beta-xylanase;
DE            Short=Xylanase;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase;
DE   Flags: Precursor;
OS   Naganishia albida (Cryptococcus albidus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Filobasidiales; Filobasidiaceae; Naganishia.
OX   NCBI_TaxID=100951;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CCY 17-4-4;
RX   PubMed=3186458; DOI=10.1093/nar/16.20.9874;
RA   Boucher F., Morosoli R., Durand S.;
RT   "Complete nucleotide sequence of the xylanase gene from the yeast
RT   Cryptococcus albidus.";
RL   Nucleic Acids Res. 16:9874-9874(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 22-93.
RA   Morosoli R., Roy C., Yaguchi M.;
RT   "Isolation and partial primary sequence of a xylanase from the yeast
RT   Cryptococcus albidus.";
RL   Biochim. Biophys. Acta 870:473-478(1986).
CC   -!- FUNCTION: Requires at least three xylose residues for catalytic
CC       activity. Does not have activity against xylobiose.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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; X12596; CAA31109.1; -; Genomic_DNA.
DR   PIR; JS0734; JS0734.
DR   AlphaFoldDB; P07529; -.
DR   SMR; P07529; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   CLAE; XYN10A_CRYAL; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   InterPro; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490; PTHR31490; 2.
DR   Pfam; PF00331; Glyco_hydro_10; 2.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           22..332
FT                   /note="Endo-1,4-beta-xylanase"
FT                   /id="PRO_0000007971"
FT   DOMAIN          26..316
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        120
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        214
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT   DISULFID        128..160
FT                   /evidence="ECO:0000250"
FT   DISULFID        247..253
FT                   /evidence="ECO:0000250"
FT   CONFLICT        88..90
FT                   /note="TGT -> AGL (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   332 AA;  35776 MW;  1814FD823E48306A CRC64;
     MLSSTTLLAI LSALALTSVQ AAPADKNSLD YLANKAGKRY LGTAVQSPQL VPGSQYVQIL
     ESQFDAITPE NEMKWEVVEP TEGNFDFTGT DKIVAEAKKT GSLLRGHNIC WDSQLRYAHE
     VAPKMKLCIN DYNIETVNAK SQAMAKVAAG LLAKGAPLHC IGMFKNAKRR SSGLLIRTAS
     SGLESHFIGG STPKDIPAAM NLFSDQGLEV PMTELDVRIP VNGNDMPANA TVAKEQVDDY
     YTSVSACLGN DLCPGVSIWQ FADPTSWIPG VFKGKLIAVS CTFSGCLLQY CVGYGAALLY
     DAQYQPKSTY YVVQQALKDG KNSGSKFHGI KL