ID   XYNA_PENCH              Reviewed;         353 AA.
AC   P29417;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   25-MAY-2022, entry version 106.
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;
GN   Name=XYLP;
OS   Penicillium chrysogenum (Penicillium notatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=5076;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10002 / CBS 277.47 / NBRC 4626 / Wis. Q-176;
RX   PubMed=8482539; DOI=10.1016/0378-1119(93)90372-a;
RA   Haas H., Friedlin E., Stoeffler G., Redl B.;
RT   "Cloning and structural organization of a xylanase-encoding gene from
RT   Penicillium chrysogenum.";
RL   Gene 126:237-242(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 61-107; 109-123; 140-146; 153-180; 199-212 AND 228-237,
RP   AND CHARACTERIZATION.
RC   STRAIN=ATCC 10002 / CBS 277.47 / NBRC 4626 / Wis. Q-176;
RX   PubMed=1420277; DOI=10.1016/0304-4165(92)90025-p;
RA   Haas H., Herfurth E., Stoeffler G., Redl B.;
RT   "Purification, characterization and partial amino acid sequences of a
RT   xylanase produced by Penicillium chrysogenum.";
RL   Biochim. Biophys. Acta 1117:279-286(1992).
CC   -!- FUNCTION: Hydrolyzes oat spelt and birchwood xylan randomly, yielding
CC       xylose and xylobiose as major end products.
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   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; M98458; AAA16427.1; -; Genomic_DNA.
DR   PIR; JN0575; JN0575.
DR   AlphaFoldDB; P29417; -.
DR   SMR; P29417; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   CLAE; XYN10A_PENCH; -.
DR   UniPathway; UPA00114; -.
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-UniPathway.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490; PTHR31490; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
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; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..353
FT                   /note="Endo-1,4-beta-xylanase"
FT                   /id="PRO_0000007975"
FT   DOMAIN          50..330
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        161
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        267
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT   CONFLICT        153
FT                   /note="L -> F (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        180
FT                   /note="E -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   353 AA;  38193 MW;  BF445C5E72FE2F94 CRC64;
     MIPNITQLKT AALVMLFAGQ ALSGPVESRQ ASESIDAKFK AHGKKYLGNI ADQGTLNGNP
     KTPAIIKANF GQLSPENSMK WDATEPSQGQ FSFAGSDYFV EFAETNGKLI RGHTLVWHSQ
     LPSWVSSITD KTTLTDVMKN HITTVMKQYK GKLYAWDVVN EIFEEDGTLR DSVFSRVLGE
     DFVRIAFETA READPEAKLY INDYNLDSAT SAKLQGMVSH VKKWIAAGVP IDGIGSQTHL
     GAGAGAAASG ALNALASAGT EEVAVTELDI AGATSTDYVD VVNACLDQPK CVGITVWGVA
     DPDSWRADES PLLFDASYNP KEAYNVSQLL SRQHAFDLYL KLGNLLLSRL HSD