ID W7A3J4_COCMI Unreviewed; 221 AA.
AC W7A3J4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Endo-1,4-beta-xylanase {ECO:0000256|ARBA:ARBA00012590, ECO:0000256|PROSITE-ProRule:PRU01097};
DE EC=3.2.1.8 {ECO:0000256|ARBA:ARBA00012590, ECO:0000256|PROSITE-ProRule:PRU01097};
GN ORFNames=COCMIDRAFT_81558 {ECO:0000313|EMBL:EUC50601.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC50601.1};
RN [1] {ECO:0000313|EMBL:EUC50601.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC50601.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000256|ARBA:ARBA00000681,
CC ECO:0000256|PROSITE-ProRule:PRU01097, ECO:0000256|RuleBase:RU362015};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000256|ARBA:ARBA00004851, ECO:0000256|PROSITE-ProRule:PRU01097,
CC ECO:0000256|RuleBase:RU362015}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000256|ARBA:ARBA00007792, ECO:0000256|PROSITE-ProRule:PRU01097,
CC ECO:0000256|RuleBase:RU362015}.
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DR EMBL; KI963922; EUC50601.1; -; Genomic_DNA.
DR RefSeq; XP_007682908.1; XM_007684718.1.
DR AlphaFoldDB; W7A3J4; -.
DR GeneID; 19125894; -.
DR KEGG; bor:COCMIDRAFT_81558; -.
DR eggNOG; ENOG502RXA7; Eukaryota.
DR HOGENOM; CLU_052631_0_0_1; -.
DR OrthoDB; 1778490at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000054032; Unassembled WGS sequence.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PROSITE-ProRule:PRU01097};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW ProRule:PRU01097};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01097};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU01097}; Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651, ECO:0000256|PROSITE-
KW ProRule:PRU01097}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..221
FT /note="Endo-1,4-beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004887488"
FT DOMAIN 31..219
FT /note="GH11"
FT /evidence="ECO:0000259|PROSITE:PS51761"
FT REGION 126..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 115
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
FT ACT_SITE 206
FT /note="Proton donor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
SQ SEQUENCE 221 AA; 23715 MW; 09DBD66837D9D657 CRC64;
MVSFTSIITA AVAATGALAA PATDVSLVAR QNTPNGEGTH NGCFWSWWSD GGARATYTNG
AGGSYSVSWG SGGNLVGGKG WNPGTARTIT YSGTYNYNGN SYLAIYGWTR NPLVEYYVVE
NFGTYDPSSQ SQNKGTVTSD GSSYKIAQST RTNQPSIDGT RTFQQYWSVR QNKRSSGSVN
MKTHFDAWAS KGMNLGQHYY QIVATEGYFS TGNAQITVSC P
//
