ID   XYNA_PIRSP              Reviewed;         625 AA.
AC   Q12667;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Endo-1,4-beta-xylanase A;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase;
DE   AltName: Full=Xylanase A;
DE            Short=XYLA;
DE   Flags: Precursor;
GN   Name=XYNA;
OS   Piromyces sp.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Piromyces; unclassified Piromyces.
OX   NCBI_TaxID=45796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7493964; DOI=10.1074/jbc.270.49.29314;
RA   Fanutti C., Ponyi T., Black G.W., Hazlewood G.P., Gilbert H.J.;
RT   "The conserved noncatalytic 40-residue sequence in cellulases and
RT   hemicellulases from anaerobic fungi functions as a protein docking
RT   domain.";
RL   J. Biol. Chem. 270:29314-29322(1995).
CC   -!- FUNCTION: Hydrolyzes 1,4-beta linked polysaccharide backbones of
CC       xylans, one of the major hemicellulose components in hardwoods and
CC       softwoods. It is more active against xylopentaose than xylotetraose,
CC       has trace activity against xylotriose. The major products released from
CC       hydrolysis of xylooligosaccharides are xylobiose and xylotriose. The
CC       reiterated 40 AA domain is involved in binding the cellulase-
CC       hemicellulase complex.
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   -!- DOMAIN: Consists of an N- and C-terminal catalytic domains linked to a
CC       middle reiterated domain. Only the C-terminal catalytic domain is
CC       active.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; X91858; CAA62969.1; -; mRNA.
DR   AlphaFoldDB; Q12667; -.
DR   SMR; Q12667; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11A_PIRSP; -.
DR   UniPathway; UPA00114; -.
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   Gene3D; 2.60.120.180; -; 2.
DR   Gene3D; 3.90.1220.10; -; 2.
DR   InterPro; IPR002883; CBM10/Dockerin_dom.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR009034; Dockerin_dom_fun_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   Pfam; PF02013; CBM_10; 2.
DR   Pfam; PF00457; Glyco_hydro_11; 2.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; SSF49899; 2.
DR   SUPFAM; SSF64571; SSF64571; 2.
DR   PROSITE; PS51763; CBM10; 2.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS51761; GH11_3; 2.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Repeat; Signal; Xylan degradation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..625
FT                   /note="Endo-1,4-beta-xylanase A"
FT                   /id="PRO_0000008017"
FT   DOMAIN          35..231
FT                   /note="GH11 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   REPEAT          259..268
FT                   /note="1"
FT   REPEAT          269..278
FT                   /note="2"
FT   DOMAIN          285..324
FT                   /note="CBM10 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT   DOMAIN          332..371
FT                   /note="CBM10 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT   DOMAIN          416..617
FT                   /note="GH11 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   REGION          245..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          255..279
FT                   /note="Linker"
FT   REGION          259..278
FT                   /note="2 X 10 AA tandem repeats of G-Q-G-[LQ]-G-N-G-Q-G-
FT                   [NQ]"
FT   REGION          374..403
FT                   /note="Linker"
FT   REGION          379..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..283
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        510
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        603
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   625 AA;  68049 MW;  9DA99B6A17290922 CRC64;
     MKLFQIFPLL LSLTSVTLAA DDFCNATGFQ GQSVVSTGHD VKKIGNIDYE QWADGGNNSA
     TFYSDGSFKC NFSNTKDYLC RSGVAFSQAK YPSEIGHIEA EYRLVKKSAS NVGYSYVGVY
     GWTLQSGISG VYEYYIVDNW LSQWRPGDWV GNTKFGDFTI DGGVYTVYKN VNGNLTQYFS
     LRKSERTCGT IDVTAHFAQW EKLGLKMPKI TEIKVLAEAG NTGGGCSGSV EIPYAKIYIN
     GKDQDGKSKG GSSSGGSNGQ GLGNGQGNGQ GQGNGQGQSA TGSGKCPSTI TSQGYKCCSS
     NCDIIYRDQS GDWGVENDEW CGCGSRVPKT TNCPSSIKNQ GYKCCSDSCE IVLTDSDGDW
     GIENDEWCGC GIKNTTPTTT TKKSNNSQPT QGQSNNNSST NTNFCSTSKH SGQSVTETSN
     KVGSIGGVGY ELWADSGNNS ATFYSDGSFS CSFRNAKDYL CRSGLSFDST KTYQQLGHMY
     ADFKLVKQNI QNVDYSYVGI YGWTRNPLVE FYVVDNWLSQ WRPGDWVGNK KHGDFTIDGA
     KYTVYENTRT GPSIDGNTTF KQYFSIRQQA RDCGTIDITA HFEQWEKLGM RMGKMHEAKV
     LGEAGSTGSG TSGTADFPYA KVYIK