3XYN_ALCSP
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 25-MAY-2022, entry version 64.
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; Proteobacteria; 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; -; 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; PTHR40079; 1.
DR Pfam; PF11606; AlcCBM31; 1.
DR SUPFAM; SSF51445; SSF51445; 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
