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Database: UniProt
Entry: V9G9B5_9BACL
LinkDB: V9G9B5_9BACL
Original site: V9G9B5_9BACL 
ID   V9G9B5_9BACL            Unreviewed;       211 AA.
AC   V9G9B5;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=JCM10914_2554 {ECO:0000313|EMBL:GAE06397.1};
OS   Paenibacillus sp. JCM 10914.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1236974 {ECO:0000313|EMBL:GAE06397.1, ECO:0000313|Proteomes:UP000018028};
RN   [1] {ECO:0000313|EMBL:GAE06397.1, ECO:0000313|Proteomes:UP000018028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10914 {ECO:0000313|EMBL:GAE06397.1,
RC   ECO:0000313|Proteomes:UP000018028};
RA   Ohkuma M., Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T.,
RA   Hattori M.;
RT   "Draft Genome Sequence of the Alkaliphilic and Xylanolytic Paenibacillus
RT   sp. Strain JCM 10914, Isolated from the Gut of a Soil-Feeding Termite.";
RL   Genome Announc. 2:e01144-13(2014).
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:GAE06397.1}.
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DR   EMBL; BAUO01000007; GAE06397.1; -; Genomic_DNA.
DR   AlphaFoldDB; V9G9B5; -.
DR   STRING; 1236974.GCA_001315105_02479; -.
DR   OrthoDB; 9806342at2; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000018028; 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:UP000018028};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651, ECO:0000256|PROSITE-
KW   ProRule:PRU01097}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..211
FT                   /note="Endo-1,4-beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004776075"
FT   DOMAIN          19..211
FT                   /note="GH11"
FT                   /evidence="ECO:0000259|PROSITE:PS51761"
FT   ACT_SITE        105
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        198
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
SQ   SEQUENCE   211 AA;  22987 MW;  E5C15991AD7EFFBD CRC64;
     MLKFGKKLMT LALAATMSFG FFATTSSAAT DYWQNWTDGG GTVNAVNGSG GNYSVNWQNT
     GNFVVGKGWN TGSPNRTVNY NAGVWAPSGN GYLTLYGWTR NSLIEYYVVD SWGTYRPTGT
     HKGTVTSDGG TYDIYTTMRY NAPSIDGTQT FAQYWSVRQS KRQTGVNSAI TFSNHVNAWS
     SKGMNLGSSW SYQVLATEGY QSSGSSNVTV W
//
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