ID   XYN1_COCCA              Reviewed;         221 AA.
AC   Q06562;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   22-FEB-2023, entry version 99.
DE   RecName: Full=Endo-1,4-beta-xylanase I;
DE            Short=Xylanase I;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 1;
DE   Flags: Precursor;
GN   Name=XYL1;
OS   Cochliobolus carbonum (Maize leaf spot fungus) (Bipolaris zeicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=5017;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Race 1 / Isolate SB111;
RX   PubMed=8400376; DOI=10.1094/mpmi-6-467;
RA   Apel P.C., Panaccione D.G., Holden F.R., Walton J.D.;
RT   "Cloning and targeted gene disruption of XYL1, a beta 1,4-xylanase gene
RT   from the maize pathogen Cochliobolus carbonum.";
RL   Mol. Plant Microbe Interact. 6:467-473(1993).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RX   AGRICOLA=IND92046127; DOI=10.1016/0885-5765(92)90070-C;
RA   Holden F.R., Walton J.D.;
RT   "Xylanases from the fungal maize pathogen Cochliobolus carbonum.";
RL   Physiol. Mol. Plant Pathol. 40:39-47(1992).
CC   -!- FUNCTION: Major xylan-degrading enzyme. Contributes to the hydrolysis
CC       of arabinoxylan, the major component of maize cell-walls.
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.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; L13596; AAA33024.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q06562; -.
DR   SMR; Q06562; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11A_COCCA; -.
DR   BRENDA; 3.2.1.8; 1551.
DR   UniPathway; UPA00114; -.
DR   PHI-base; PHI:571; -.
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   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033119; GH11_AS_2.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   PANTHER; PTHR46828:SF3; ENDO-1,4-BETA-XYLANASE; 1.
DR   PANTHER; PTHR46828; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 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..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..221
FT                   /note="Endo-1,4-beta-xylanase I"
FT                   /id="PRO_0000008003"
FT   DOMAIN          31..219
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   REGION          126..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        115
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        206
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT   CONFLICT        81
FT                   /note="W -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        107
FT                   /note="G -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        131
FT                   /note="S -> W (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   221 AA;  23728 MW;  59DBD8983FC5B08C CRC64;
     MVSFTSIITA AVAATGALAA PATDVSLVAR QNTPNGEGTH NGCFWSWWSD GGARATYTNG
     AGGSYSVSWG SGGNLVGGKG WNPGTARTIT YSGTYNYNGN SYLAVYGWTR NPLVEYYVVE
     NFGTYDPSSQ SQNKGTVTSD GSSYKIAQST RTNQPSIDGT RTFQQYWSVR QNKRSSGSVN
     MKTHFDAWAS KGMNLGQHYY QIVATEGYFS TGNAQITVNC P
//