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Database: UniProt
Entry: V9TXH2
LinkDB: V9TXH2
Original site: V9TXH2 
ID   XYN11_PAEBA             Reviewed;         210 AA.
AC   V9TXH2;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   13-FEB-2019, entry version 30.
DE   RecName: Full=Endo-1,4-beta-xylanase Xyn11E {ECO:0000303|PubMed:24549767};
DE            EC=3.2.1.8 {ECO:0000269|PubMed:24549767};
DE   Flags: Precursor;
GN   Name=xyn11E {ECO:0000303|PubMed:24549767,
GN   ECO:0000312|EMBL:AHC74025.1};
GN   ORFNames=DFQ00_11065 {ECO:0000312|EMBL:PYE48003.1};
OS   Paenibacillus barcinonensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=198119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP   BIOTECHNOLOGY.
RC   STRAIN=DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23;
RX   PubMed=24549767; DOI=10.1007/s00253-014-5565-2;
RA   Valenzuela S.V., Diaz P., Pastor F.I.;
RT   "Xyn11E from Paenibacillus barcinonensis BP-23: a LppX-chaperone-
RT   dependent xylanase with potential for upgrading paper pulps.";
RL   Appl. Microbiol. Biotechnol. 98:5949-5957(2014).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23;
RX   PubMed=26203337; DOI=10.1186/s40793-015-0017-x;
RA   Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA   De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA   Kyrpides N.C.;
RT   "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase
RT   III: the genomes of soil and plant-associated and newly described type
RT   strains.";
RL   Stand. Genomic Sci. 10:26-26(2015).
CC   -!- FUNCTION: Involved in depolymerization of xylan, a major component
CC       of the lignocellulosic substrates. Acts as an endo-xylanase that
CC       efficiently hydrolyzes the beta-1,4 glycosidic linkages between
CC       the xylopyranosyl residues in the main chain of the polymer,
CC       leading to the degradation of xylan into short oligosaccharides.
CC       Shows high activity toward branched xylans from both softwoods
CC       (arabinoxylans) and hardwoods (glucuronoxylans), showing the
CC       highest activity on beechwood xylan. Also hydrolyzes long
CC       xylooligosaccharides (with a degree of polymerization of greater
CC       than or equal to 5), while oligomers shorter than xylotetraose are
CC       not degraded. Is not active on carboxymethyl cellulose (CMC),
CC       Avicel, starch, polygalacturonic acid, laminarin, pectin, beta-D-
CC       barley glucan, or lichenan. {ECO:0000269|PubMed:24549767}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8; Evidence={ECO:0000269|PubMed:24549767};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=12.98 mg/ml for beechwood xylan
CC         {ECO:0000269|PubMed:24549767};
CC         Vmax=3023 umol/min/mg enzyme for the hydrolysis of beechwood
CC         xylan {ECO:0000269|PubMed:24549767};
CC       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:24549767};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius. Retains about 80% of
CC         the activity after incubation for 2 hours at 50 degrees Celsius,
CC         but is rapidly inactivated at higher temperatures.
CC         {ECO:0000269|PubMed:24549767};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000269|PubMed:24549767}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24549767}.
CC   -!- BIOTECHNOLOGY: This enzyme liberates reducing sugars from
CC       elemental chlorine free (ECF) and totally chlorine free (TCF)
CC       bleached pulps from eucalyptus, sisal, and flax, which makes it a
CC       good candidate for the enzymatic-assisted production of high-
CC       cellulose-content pulps from paper-grade pulps.
CC       {ECO:0000269|PubMed:24549767}.
CC   -!- MISCELLANEOUS: Is dependent on P.barcinonensis lipoprotein LppX
CC       for its expression in an active form.
CC       {ECO:0000269|PubMed:24549767}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; KF766535; AHC74025.1; -; Genomic_DNA.
DR   EMBL; QJSW01000010; PYE48003.1; -; Genomic_DNA.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000247790; Unassembled WGS sequence.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IDA:UniProtKB.
DR   GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
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   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; SSF49899; 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   Carbohydrate metabolism; Complete proteome; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    210       Endo-1,4-beta-xylanase Xyn11E.
FT                                /FTId=PRO_5016557792.
FT   DOMAIN       24    210       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    104    104       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097, ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    197    197       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097, ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
SQ   SEQUENCE   210 AA;  23145 MW;  E3454EC152DFEB41 CRC64;
     MFKFGKKLMT VVLAASMSFG VFAATTGATD YWQNWTDGGG TVNAVNGSGG NYSVNWQNTG
     NFVVGKGWTY GTPNRVVNYN AGVFSPSGNG YLTFYGWTRN ALIEYYVVDN WGTYRPTGTY
     KGTVNSDGGT YDIYTTMRYN QPSIDGYSTF PQYWSVRQSK RPIGVNSQIT FQNHVNAWAS
     KGMNLGSSWS YQVLATEGYQ SSGSSNVTVW
//
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