ID   Q7SIE3_SALAG            Unreviewed;       207 AA.
AC   Q7SIE3;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   03-MAY-2023, entry version 109.
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};
OS   Salipaludibacillus agaradhaerens (Bacillus agaradhaerens).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX   NCBI_TaxID=76935 {ECO:0000313|PDB:1H4G};
RN   [1] {ECO:0007829|PDB:1H4G, ECO:0007829|PDB:1QH6}
RP   X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 2-207, PYRROLIDONE CARBOXYLIC
RP   ACID AT GLN-1, AND ACTIVE SITE.
RX   PubMed=10381409; DOI=10.1016/S1074-5521(99)80066-0;
RA   Sabini E., Sulzenbacher G., Dauter M., Dauter Z., Jorgensen P.L.,
RA   Schulein M., Dupont C., Davies G.J., Wilson K.S.;
RT   "Catalysis and specificity in enzymatic glycoside hydrolysis: a 2,5B
RT   conformation for the glycosyl-enzyme intermediate revealed by the structure
RT   of the Bacillus agaradhaerens family 11 xylanase.";
RL   Chem. Biol. 6:483-492(1999).
RN   [2] {ECO:0007829|PDB:2F6B}
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-206.
RA   Balakrishnan H., Satyanarayana L., Gaikward S., Suresh C.G.;
RT   "Structural and active site modification studies implicate Glu, Trp and Arg
RT   in the activity of xylanase from alkalophilic Bacillus sp. (NCL 87-6-10).";
RL   Submitted (NOV-2005) to the PDB data bank.
RN   [3] {ECO:0007829|PDB:2NQY}
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-206.
RA   Satyanarayana L., Gaikwad S.M., Balakrishnan H., Suresh C.G.;
RT   "Crystal structure of alkaline thermophlic xylanase from Bacillus sp. (NCL
RT   86-6-10) with complex xylotriose: Xylotriose cleaved to xylobiose and
RT   xylose.";
RL   Submitted (NOV-2006) to the PDB data bank.
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}.
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DR   PDB; 1H4G; X-ray; 1.10 A; A/B=1-207.
DR   PDB; 1QH6; X-ray; 2.00 A; A/B=1-207.
DR   PDB; 1QH7; X-ray; 1.78 A; A/B=1-207.
DR   PDB; 2F6B; X-ray; 2.80 A; A/B=2-206.
DR   PDB; 2NQY; X-ray; 2.40 A; A/B=1-206.
DR   PDBsum; 1H4G; -.
DR   PDBsum; 1QH6; -.
DR   PDBsum; 1QH7; -.
DR   PDBsum; 2F6B; -.
DR   PDBsum; 2NQY; -.
DR   AlphaFoldDB; Q7SIE3; -.
DR   SMR; Q7SIE3; -.
DR   UniPathway; UPA00114; -.
DR   EvolutionaryTrace; Q7SIE3; -.
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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1H4G, ECO:0007829|PDB:1QH6};
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   Pyrrolidone carboxylic acid {ECO:0007829|PDB:1H4G};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651, ECO:0000256|PROSITE-
KW   ProRule:PRU01097}.
FT   DOMAIN          2..197
FT                   /note="GH11"
FT                   /evidence="ECO:0000259|PROSITE:PS51761"
FT   ACT_SITE        94
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        184
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0007829|PDB:1H4G"
SQ   SEQUENCE   207 AA;  23152 MW;  C498EF0D0A085D0B CRC64;
     QIVTDNSIGN HDGYDYEFWK DSGGSGTMIL NHGGTFSAQW NNVNNILFRK GKKFNETQTH
     QQVGNMSINY GANFQPNGNA YLCVYGWTVD PLVEYYIVDS WGNWRPPGAT PKGTITVDGG
     TYDIYETLRV NQPSIKGIAT FKQYWSVRRS KRTSGTISVS NHFRAWENLG MNMGKMYEVA
     LTVEGYQSSG SANVYSNTLR INGNPLS
//