XYN11_PAEBA
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 25-MAY-2022, entry version 35.
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, ECO:0000312|EMBL:AHC74025.1};
GN ORFNames=DFQ00_11065 {ECO:0000312|EMBL:PYE48003.1};
OS Paenibacillus barcinonensis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=198119;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND 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-dependent
RT 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 III:
RT 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 of
CC the lignocellulosic substrates. Acts as an endo-xylanase that
CC efficiently hydrolyzes the beta-1,4 glycosidic linkages between the
CC xylopyranosyl residues in the main chain of the polymer, leading to the
CC degradation of xylan into short oligosaccharides. Shows high activity
CC toward branched xylans from both softwoods (arabinoxylans) and
CC hardwoods (glucuronoxylans), showing the highest activity on beechwood
CC xylan. Also hydrolyzes long xylooligosaccharides (with a degree of
CC polymerization of greater than or equal to 5), while oligomers shorter
CC than xylotetraose are not degraded. Is not active on carboxymethyl
CC cellulose (CMC), Avicel, starch, polygalacturonic acid, laminarin,
CC pectin, beta-D-barley glucan, or lichenan.
CC {ECO:0000269|PubMed:24549767}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC 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 {ECO:0000269|PubMed:24549767};
CC Vmax=3023 umol/min/mg enzyme for the hydrolysis of beechwood xylan
CC {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 the
CC activity after incubation for 2 hours at 50 degrees Celsius, but is
CC 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 elemental
CC chlorine free (ECF) and totally chlorine free (TCF) bleached pulps from
CC eucalyptus, sisal, and flax, which makes it a good candidate for the
CC enzymatic-assisted production of high-cellulose-content pulps from
CC paper-grade pulps. {ECO:0000269|PubMed:24549767}.
CC -!- MISCELLANEOUS: Is dependent on P.barcinonensis lipoprotein LppX for its
CC expression in an active form. {ECO:0000269|PubMed:24549767}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; KF766535; AHC74025.1; -; Genomic_DNA.
DR EMBL; QJSW01000010; PYE48003.1; -; Genomic_DNA.
DR AlphaFoldDB; V9TXH2; -.
DR SMR; V9TXH2; -.
DR EnsemblBacteria; PYE48003; PYE48003; DFQ00_11065.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000247790; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..210
FT /note="Endo-1,4-beta-xylanase Xyn11E"
FT /id="PRO_5016557792"
FT DOMAIN 24..210
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 104
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097,
FT ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097,
FT ECO:0000255|PROSITE-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
