ID L7EST2_9ACTN Unreviewed; 229 AA.
AC L7EST2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=STRTUCAR8_09892 {ECO:0000313|EMBL:ELP61954.1};
OS Streptomyces turgidiscabies Car8.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP61954.1, ECO:0000313|Proteomes:UP000010931};
RN [1] {ECO:0000313|EMBL:ELP61954.1, ECO:0000313|Proteomes:UP000010931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Car8 {ECO:0000313|EMBL:ELP61954.1,
RC ECO:0000313|Proteomes:UP000010931};
RX PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT "Streptomyces turgidiscabies Car8 contains a modular pathogenicity island
RT that shares virulence genes with other actinobacterial plant pathogens.";
RL Plasmid 65:118-124(2011).
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|PROSITE-ProRule:PRU01097, ECO:0000256|RuleBase:RU362015}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELP61954.1}.
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DR EMBL; AEJB01000646; ELP61954.1; -; Genomic_DNA.
DR RefSeq; WP_006383158.1; NZ_AEJB01000646.1.
DR AlphaFoldDB; L7EST2; -.
DR STRING; 85558.T45_08524; -.
DR PATRIC; fig|698760.3.peg.9090; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000010931; 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; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR PANTHER; PTHR46828:SF2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000010931};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651, ECO:0000256|PROSITE-
KW ProRule:PRU01097}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..229
FT /note="Endo-1,4-beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003972868"
FT DOMAIN 42..229
FT /note="GH11"
FT /evidence="ECO:0000259|PROSITE:PS51761"
FT ACT_SITE 126
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
FT ACT_SITE 216
FT /note="Proton donor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
SQ SEQUENCE 229 AA; 24756 MW; 0F6569ED89FE1FA0 CRC64;
MKSAPAPVSA SRLRLLISGV CTMLLVAVAA LTLPTTAQAA TVVTTNQTGT NNGYYYSFWT
DAPGTVSMTL NSGGNYSTSW SNTGNFVAGK GWSNGSRRTV RYSGSFNPSG NAYLALYGWT
SNPLVEYYIV DNWGTYRPTG TYKGTVTSDG GTYDIYQTTR YNAPSVEGTR TFNQYWSVRQ
SKRTGGTITT GNHFDAWARA GMPMGSFNYY MILATEGYRS SGNSNITVG
//
