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   31-MAY-2011, entry version 64.
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 (Bipolaris zeicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Pleosporaceae; Cochliobolus.
OX   NCBI_TaxID=5017;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Race 1 / Isolate SB111;
RX   MEDLINE=94003417; PubMed=8400376;
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
RT   gene 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
CC       hydrolysis of arabinoxylan, the major component of maize cell-
CC       walls.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-xylosidic
CC       linkages in xylans.
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)
CC       family.
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DR   EMBL; L13596; AAA33024.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q06562; -.
DR   SMR; Q06562; 31-218.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   BRENDA; 3.2.1.8; 1551.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   InterPro; IPR013319; Glyco_hydro_11/12_cat.
DR   InterPro; IPR018208; Glyco_hydro_11_AS.
DR   Gene3D; G3DSA:2.60.120.180; Glyco_hydro_11/12_cat; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   PROSITE; PS00776; GLYCOSYL_HYDROL_F11_1; 1.
DR   PROSITE; PS00777; GLYCOSYL_HYDROL_F11_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     30       Potential.
FT   CHAIN        31    221       Endo-1,4-beta-xylanase I.
FT                                /FTId=PRO_0000008003.
FT   ACT_SITE    115    115       Nucleophile (By similarity).
FT   ACT_SITE    206    206       Proton donor (By similarity).
FT   CONFLICT     81     81       W -> I (in Ref. 2; AA sequence).
FT   CONFLICT    107    107       G -> A (in Ref. 2; AA sequence).
FT   CONFLICT    131    131       S -> W (in Ref. 2; AA sequence).
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
//