ID   3XYN_ALCSP              Reviewed;         469 AA.
AC   Q8RS40;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-MAY-2023, entry version 67.
DE   RecName: Full=Beta-1,3-xylanase {ECO:0000312|EMBL:BAB88993.1};
DE            EC=3.2.1.32;
DE   Flags: Precursor;
GN   Name=txyA {ECO:0000303|PubMed:11948152};
GN   Synonyms=3xynAlc {ECO:0000312|EMBL:BAB88993.1};
OS   Alcaligenes sp.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Alcaligenes.
OX   NCBI_TaxID=512;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAB88993.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND CBM31 DOMAIN.
RC   STRAIN=XY-234 {ECO:0000312|EMBL:BAB88993.1};
RX   PubMed=11948152; DOI=10.1128/jb.184.9.2399-2403.2002;
RA   Okazaki F., Tamaru Y., Hashikawa S., Li Y.T., Araki T.;
RT   "Novel carbohydrate-binding module of beta-1,3-xylanase from a marine
RT   bacterium, Alcaligenes sp. strain XY-234.";
RL   J. Bacteriol. 184:2399-2403(2002).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 23-35, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC   STRAIN=XY-234 {ECO:0000269|PubMed:12501421};
RX   PubMed=12501421; DOI=10.2323/jgam.44.269;
RA   Araki T., Inoue N., Morishita T.;
RT   "Purification and characterization of beta-1,3-xylanase from a marine
RT   bacterium, Alcaligenes sp. XY-234.";
RL   J. Gen. Appl. Microbiol. 44:269-274(1998).
RN   [3] {ECO:0000305}
RP   X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 375-469, AND DISULFIDE BONDS.
RC   STRAIN=XY-234 {ECO:0000269|PubMed:16061225};
RX   PubMed=16061225; DOI=10.1016/j.febslet.2005.06.062;
RA   Hashimoto H., Tamai Y., Okazaki F., Tamaru Y., Shimizu T., Araki T.,
RA   Sato M.;
RT   "The first crystal structure of a family 31 carbohydrate-binding module
RT   with affinity to beta-1,3-xylan.";
RL   FEBS Lett. 579:4324-4328(2005).
CC   -!- FUNCTION: Catalyzes the hydrolysis of beta-1,3-xylan into
CC       oligosaccharides, mainly xylotriose and xylobiose with smaller amounts
CC       of xylotetraose, xylose, xylopentaose and xylohexaose. Does not
CC       hydrolyze xylobiose, p-nitrophenyl-beta-xyloside, beta-1,4-xylan,
CC       carboxymethylcellulose, curdlan, glucomannan or beta-1,4-mannan.
CC       {ECO:0000269|PubMed:11948152, ECO:0000269|PubMed:12501421}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->3)-beta-D-glycosidic linkages in
CC         (1->3)-beta-D-xylans.; EC=3.2.1.32;
CC         Evidence={ECO:0000269|PubMed:11948152, ECO:0000269|PubMed:12501421};
CC   -!- ACTIVITY REGULATION: Completely inhibited by CuCl(2), FeCl(3), HgCl(2)
CC       and N-bromosuccinimide. Moderately inhibited by AgCl, AlCl(3),
CC       Pb(CH(3)COO)(2) and dithiothreitol. BaCl(2), CaCl(2), KCl, MgCl(2),
CC       MnCl(2), NaCl, ZnCl(2), ethylenediaminetetraacetic acid, N-
CC       ethylmaleimide, iodoacetic acid and p-chloromercuribenzoic acid have
CC       little or no effect on activity. {ECO:0000269|PubMed:12501421}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0-7.5. Stable from pH 5.0-11.0. Retains 65% and 70%
CC         of activity respectively when incubated at pH 4.0 and 12.0 for 24
CC         hours. {ECO:0000269|PubMed:11948152, ECO:0000269|PubMed:12501421};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius. Stable below 40 degrees
CC         Celsius. Loses 70% and 99% of activity respectively when incubated
CC         for 10 minutes at 50 and 60 degrees Celsius.
CC         {ECO:0000269|PubMed:11948152, ECO:0000269|PubMed:12501421};
CC   -!- INDUCTION: By beta-1,3-xylan. {ECO:0000269|PubMed:12501421}.
CC   -!- DOMAIN: The carbohydrate binding module (CBM) binds to insoluble beta-
CC       1,3-xylan, but not to insoluble beta-1,4-xylan, beta-1,4-glucan, beta-
CC       1,4-mannan, curdlan, chitin, or soluble polysaccharides.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01100}.
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DR   EMBL; AB039953; BAB88993.1; -; Genomic_DNA.
DR   PDB; 2COV; X-ray; 1.25 A; D/E/F/G/H/I=375-469.
DR   PDBsum; 2COV; -.
DR   AlphaFoldDB; Q8RS40; -.
DR   SMR; Q8RS40; -.
DR   CAZy; CBM31; Carbohydrate-Binding Module Family 31.
DR   CAZy; GH26; Glycoside Hydrolase Family 26.
DR   KEGG; ag:BAB88993; -.
DR   BRENDA; 3.2.1.32; 236.
DR   EvolutionaryTrace; Q8RS40; -.
DR   GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IDA:UniProtKB.
DR   GO; GO:0033914; F:xylan 1,3-beta-xylosidase activity; IDA:UniProtKB.
DR   GO; GO:0033905; F:xylan endo-1,3-beta-xylosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006080; P:substituted mannan metabolic process; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
DR   Gene3D; 2.60.40.2450; Beta-1,3-xylanase, CBM31 domain; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR021016; Beta-xylanase.
DR   InterPro; IPR038560; Beta-xylanase_CBM31_sf.
DR   InterPro; IPR022790; GH26_dom.
DR   InterPro; IPR000805; Glyco_hydro_26.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR40079:SF4; GH26 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR40079; MANNAN ENDO-1,4-BETA-MANNOSIDASE E-RELATED; 1.
DR   Pfam; PF11606; AlcCBM31; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51764; GH26; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Signal; Xylan degradation.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:12501421"
FT   CHAIN           23..469
FT                   /note="Beta-1,3-xylanase"
FT                   /evidence="ECO:0000269|PubMed:12501421"
FT                   /id="PRO_0000403219"
FT   DOMAIN          23..293
FT                   /note="GH26"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   REGION          352..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..469
FT                   /note="Carbohydrate binding module (CBM)"
FT   ACT_SITE        138
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   ACT_SITE        234
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   DISULFID        382..468
FT                   /evidence="ECO:0000269|PubMed:16061225"
FT   DISULFID        413..418
FT                   /evidence="ECO:0000269|PubMed:16061225"
FT   HELIX           380..382
FT                   /evidence="ECO:0007829|PDB:2COV"
FT   STRAND          384..392
FT                   /evidence="ECO:0007829|PDB:2COV"
FT   STRAND          395..401
FT                   /evidence="ECO:0007829|PDB:2COV"
FT   STRAND          408..414
FT                   /evidence="ECO:0007829|PDB:2COV"
FT   STRAND          417..420
FT                   /evidence="ECO:0007829|PDB:2COV"
FT   STRAND          422..424
FT                   /evidence="ECO:0007829|PDB:2COV"
FT   STRAND          427..433
FT                   /evidence="ECO:0007829|PDB:2COV"
FT   STRAND          439..448
FT                   /evidence="ECO:0007829|PDB:2COV"
FT   TURN            449..452
FT                   /evidence="ECO:0007829|PDB:2COV"
FT   STRAND          453..462
FT                   /evidence="ECO:0007829|PDB:2COV"
SQ   SEQUENCE   469 AA;  52257 MW;  B61058CE40353F58 CRC64;
     MKKLAKMISI ATLGACAFSA HALDGKLVPN EGVLVSVGQD VDSVNDYSSA MSTTPAGVTN
     YVGIVNLDGL ASNADAGAGR NNVVELANLY PTSALIVGVS MNGQIQNVAQ GQYNANIDTL
     IQTLGELDRP VYLRWAYEVD GPWNGHNTED LKQSFRNVYQ RIRELGYGDN ISMIWQVASY
     CPTAPGQLSS WWPGDDVVDW VGLSYFAPQD CNWDRVNEAA QWARSHNKPL FINESSPQRY
     QLADRTYSSD PAKGTNRQSK TEQQIWSEWF APYFQFMEDN KDILKGFTYI NADWDSQWRW
     AAPYNEGYWG DSRVQVLPYI KQQWQDTLEN PKFINHSSDL FAKLGYVADG GDNGGDNGGD
     NGGDNGGDNG GDNGGTEPPE NCQDDFNFNY VSDQEIEVYH VDKGWSAGWN YVCLNDYCLP
     GNKSNGAFRK TFNAVLGQDY KLTFKVEDRY GQGQQILDRN ITFTTQVCN
//