GenomeNet

Database: UniProt
Entry: O69231
LinkDB: O69231
Original site: O69231 
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   12-SEP-2018, entry version 69.
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;
OC   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
RT   high activity on aryl-xylosides: a new subclass of family 10
RT   xylanases.";
RL   Appl. Microbiol. Biotechnol. 61:226-233(2003).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY
RP   REGULATION, 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
CC       the hydrolysis of short xylooligosaccharides resulting from
CC       extracellular xylan hydrolysis, once they have been transported
CC       inside cells. Shows similar activity on xylans of different rate
CC       of arabinose or methylglucuronic substitution. Also displays high
CC       activity on aryl-xylosides. Is active on xylotetraose and
CC       xylotriose, but does not hydrolyze xylobiose, indicating that XynB
CC       is a xylanase and not a beta-xylosidase.
CC       {ECO:0000269|PubMed:12698280, ECO:0000269|PubMed:8998999}.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-xylosidic
CC       linkages in xylans. {ECO:0000269|PubMed:12698280,
CC       ECO:0000269|PubMed:8998999}.
CC   -!- ACTIVITY REGULATION: Completely inhibited by Ag(2+), Cu(2+),
CC       Hg(2+), Mn(2+), Pb(2+) and Sn(2+). Strongly inhibited by Fe(2+)
CC       and Zn(2+). Co(2+) and Ni(2+) cause little inhibition while Ca(2+)
CC       and Mg(2+) do not affect enzyme activity, and Ba(2+) produces a
CC       small stimulating effect. Irreversibly inactivated by SDS in
CC       vitro. {ECO:0000269|PubMed:8998999}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5. Shows more than 75% of maximum activity from
CC         pH 5 to 10. Is still active at pH 12.
CC         {ECO:0000269|PubMed:8998999};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius. Loses 100% activity
CC         after 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}.
CC       Note=Is not secreted to the medium but instead remains cell-
CC       associated, in the soluble fraction, even in late stationary-phase
CC       cultures.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F)
CC       family. Cytoplasmic xylanase subfamily. {ECO:0000305}.
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   ProteinModelPortal; 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; IPR001000; GH10.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
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      1       Removed. {ECO:0000269|PubMed:12698280}.
FT   CHAIN         2    332       Endo-1,4-beta-xylanase B.
FT                                /FTId=PRO_0000366196.
FT   DOMAIN        2    331       GH10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01096}.
FT   ACT_SITE    134    134       Proton donor. {ECO:0000250}.
FT   ACT_SITE    241    241       Nucleophile. {ECO:0000250}.
FT   HELIX        10     12       {ECO:0000244|PDB:3EMZ}.
FT   TURN         13     15       {ECO:0000244|PDB:3EMZ}.
FT   STRAND       17     22       {ECO:0000244|PDB:3EMZ}.
FT   HELIX        24     37       {ECO:0000244|PDB:3EMZ}.
FT   STRAND       39     45       {ECO:0000244|PDB:3EMZ}.
FT   HELIX        49     52       {ECO:0000244|PDB:3EMZ}.
FT   STRAND       54     57       {ECO:0000244|PDB:3EMQ}.
FT   HELIX        62     72       {ECO:0000244|PDB:3EMZ}.
FT   TURN         73     75       {ECO:0000244|PDB:3EMZ}.
FT   STRAND       77     80       {ECO:0000244|PDB:3EMZ}.
FT   STRAND       86     88       {ECO:0000244|PDB:3EMZ}.
FT   HELIX        91     94       {ECO:0000244|PDB:3EMZ}.
FT   STRAND       99    101       {ECO:0000244|PDB:3EMZ}.
FT   HELIX       104    121       {ECO:0000244|PDB:3EMZ}.
FT   TURN        122    125       {ECO:0000244|PDB:3EMZ}.
FT   STRAND      127    133       {ECO:0000244|PDB:3EMZ}.
FT   HELIX       148    152       {ECO:0000244|PDB:3EMZ}.
FT   HELIX       157    168       {ECO:0000244|PDB:3EMZ}.
FT   STRAND      172    180       {ECO:0000244|PDB:3EMZ}.
FT   HELIX       184    199       {ECO:0000244|PDB:3EMZ}.
FT   STRAND      206    209       {ECO:0000244|PDB:3EMZ}.
FT   STRAND      212    214       {ECO:0000244|PDB:3EMZ}.
FT   HELIX       220    231       {ECO:0000244|PDB:3EMZ}.
FT   TURN        232    234       {ECO:0000244|PDB:3EMC}.
FT   STRAND      236    247       {ECO:0000244|PDB:3EMZ}.
FT   HELIX       261    280       {ECO:0000244|PDB:3EMZ}.
FT   TURN        281    284       {ECO:0000244|PDB:3EMZ}.
FT   STRAND      285    294       {ECO:0000244|PDB:3EMZ}.
FT   HELIX       299    301       {ECO:0000244|PDB:3EMZ}.
FT   STRAND      302    305       {ECO:0000244|PDB:3EMZ}.
FT   STRAND      313    315       {ECO:0000244|PDB:3EMZ}.
FT   HELIX       323    328       {ECO:0000244|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
//
DBGET integrated database retrieval system