XYNB_PAEBA
ID XYNB_PAEBA Reviewed; 332 AA.
AC O69231;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Endo-1,4-beta-xylanase B;
DE Short=Xylanase B;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase B;
GN Name=xynB;
OS Paenibacillus barcinonensis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=198119;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23;
RX PubMed=12698280; DOI=10.1007/s00253-003-1239-1;
RA Gallardo O., Diaz P., Pastor F.I.J.;
RT "Characterization of a Paenibacillus cell-associated xylanase with high
RT activity on aryl-xylosides: a new subclass of family 10 xylanases.";
RL Appl. Microbiol. Biotechnol. 61:226-233(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23;
RX PubMed=8998999; DOI=10.1111/j.1574-6968.1996.tb08120.x;
RA Blanco A., Diaz P., Martinez J., Lopez O., Soler C., Pastor F.I.J.;
RT "Cloning of a Bacillus sp. BP-23 gene encoding a xylanase with high
RT activity against aryl xylosides.";
RL FEMS Microbiol. Lett. 137:285-290(1996).
CC -!- FUNCTION: Plays a role in plant xylan biodegradation, probably via the
CC hydrolysis of short xylooligosaccharides resulting from extracellular
CC xylan hydrolysis, once they have been transported inside cells. Shows
CC similar activity on xylans of different rate of arabinose or
CC methylglucuronic substitution. Also displays high activity on aryl-
CC xylosides. Is active on xylotetraose and xylotriose, but does not
CC hydrolyze xylobiose, indicating that XynB is a xylanase and not a beta-
CC xylosidase. {ECO:0000269|PubMed:12698280, ECO:0000269|PubMed:8998999}.
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:12698280,
CC ECO:0000269|PubMed:8998999};
CC -!- ACTIVITY REGULATION: Completely inhibited by Ag(2+), Cu(2+), Hg(2+),
CC Mn(2+), Pb(2+) and Sn(2+). Strongly inhibited by Fe(2+) and Zn(2+).
CC Co(2+) and Ni(2+) cause little inhibition while Ca(2+) and Mg(2+) do
CC not affect enzyme activity, and Ba(2+) produces a small stimulating
CC effect. Irreversibly inactivated by SDS in vitro.
CC {ECO:0000269|PubMed:8998999}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5. Shows more than 75% of maximum activity from pH 5
CC to 10. Is still active at pH 12. {ECO:0000269|PubMed:8998999};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius. Loses 100% activity after
CC incubation for 15 minutes at 50 degrees Celsius.
CC {ECO:0000269|PubMed:8998999};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12698280}. Note=Is
CC not secreted to the medium but instead remains cell-associated, in the
CC soluble fraction, even in late stationary-phase cultures.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC Cytoplasmic xylanase subfamily. {ECO:0000305}.
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DR EMBL; AJ006646; CAA07174.1; -; Genomic_DNA.
DR PDB; 3EMC; X-ray; 2.10 A; A=2-332.
DR PDB; 3EMQ; X-ray; 2.73 A; A=2-332.
DR PDB; 3EMZ; X-ray; 2.08 A; A=2-332.
DR PDBsum; 3EMC; -.
DR PDBsum; 3EMQ; -.
DR PDBsum; 3EMZ; -.
DR AlphaFoldDB; O69231; -.
DR SMR; O69231; -.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR UniPathway; UPA00114; -.
DR EvolutionaryTrace; O69231; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490; PTHR31490; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm;
KW Direct protein sequencing; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Xylan degradation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12698280"
FT CHAIN 2..332
FT /note="Endo-1,4-beta-xylanase B"
FT /id="PRO_0000366196"
FT DOMAIN 2..331
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 134
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 241
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:3EMZ"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:3EMZ"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:3EMZ"
FT HELIX 24..37
FT /evidence="ECO:0007829|PDB:3EMZ"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:3EMZ"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:3EMZ"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:3EMQ"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:3EMZ"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:3EMZ"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:3EMZ"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3EMZ"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:3EMZ"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:3EMZ"
FT HELIX 104..121
FT /evidence="ECO:0007829|PDB:3EMZ"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:3EMZ"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:3EMZ"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:3EMZ"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:3EMZ"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:3EMZ"
FT HELIX 184..199
FT /evidence="ECO:0007829|PDB:3EMZ"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:3EMZ"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:3EMZ"
FT HELIX 220..231
FT /evidence="ECO:0007829|PDB:3EMZ"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:3EMC"
FT STRAND 236..247
FT /evidence="ECO:0007829|PDB:3EMZ"
FT HELIX 261..280
FT /evidence="ECO:0007829|PDB:3EMZ"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:3EMZ"
FT STRAND 285..294
FT /evidence="ECO:0007829|PDB:3EMZ"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:3EMZ"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:3EMZ"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:3EMZ"
FT HELIX 323..328
FT /evidence="ECO:0007829|PDB:3EMZ"
SQ SEQUENCE 332 AA; 38561 MW; DDEF7BCF17C8A72E CRC64;
MSTEIPSLSA SYANSFKIGA AVHTRMLQTE GEFIAKHYNS VTAENQMKFE EVHPREHEYT
FEAADEIVDF AVARGIGVRG HTLVWHNQTP AWMFEDASGG TASREMMLSR LKQHIDTVVG
RYKDQIYAWD VVNEAIEDKT DLIMRDTKWL RLLGEDYLVQ AFNMAHEADP NALLFYNDYN
ETDPVKREKI YNLVRSLLDQ GAPVHGIGMQ GHWNIHGPSM DEIRQAIERY ASLDVQLHVT
ELDLSVFRHE DQRTDLTEPT AEMAELQQKR YEDIFGLFRE YRSNITSVTF WGVADNYTWL
DNFPVRGRKN WPFVFDTELQ PKDSFWRIIG QD
