ID 3XYN2_VIBSX Reviewed; 460 AA. AC Q9LCB9; DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 13-SEP-2023, entry version 71. DE RecName: Full=Beta-1,3-xylanase TXYA; DE EC=3.2.1.32; DE AltName: Full=Endo-1,3-beta-xylanase {ECO:0000312|EMBL:BAA94698.1}; DE Flags: Precursor; GN Name=txyA {ECO:0000312|EMBL:BAA94698.1}; OS Vibrio sp. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=678; RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA94698.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-41 AND 300-313, RP FUNCTION, AND CATALYTIC ACTIVITY. RC STRAIN=XY-214 {ECO:0000312|EMBL:BAA94698.1}; RX PubMed=10742274; DOI=10.1128/aem.66.4.1741-1743.2000; RA Araki T., Hashikawa S., Morishita T.; RT "Cloning, sequencing, and expression in Escherichia coli of the new gene RT encoding beta-1,3-xylanase from a marine bacterium, Vibrio sp. strain XY- RT 214."; RL Appl. Environ. Microbiol. 66:1741-1743(2000). RN [2] {ECO:0000305} RP PROTEIN SEQUENCE OF 23-38, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION. RC STRAIN=XY-214 {ECO:0000269|PubMed:10635569}; RX PubMed=10635569; DOI=10.1271/bbb.63.2017; RA Araki T., Tani S., Maeda K., Hashikawa S., Nakagawa H., Morishita T.; RT "Purification and characterization of beta-1,3-xylanase from a marine RT bacterium, Vibrio sp. XY-214."; RL Biosci. Biotechnol. Biochem. 63:2017-2019(1999). 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. Weakly active CC toward beta-1,3-xylotriose, yielding xylose and xylobiose. Converts CC beta-1,3-xylotetraose into xylotriose, xylobiose and xylose. Converts CC beta-1,3-xylopentaose into xylotetraose, xylotriose, xylobiose and CC xylose. Does not hydrolyze xylobiose, p-nitrophenyl-beta-xyloside, CC beta-1,4-xylan, curdlan or carboxymethylcellulose. CC {ECO:0000269|PubMed:10635569, ECO:0000269|PubMed:10742274}. 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:10635569, ECO:0000269|PubMed:10742274}; CC -!- ACTIVITY REGULATION: Completely inhibited by Cu(2+), Hg(2+) and N- CC bromosuccinimide. Strongly inhibited by Ag(+), Zn(2+) and Pb(2+). CC Moderately inhibited by Fe(3+), Al(3+), Mn(2+), dithiothreitol and p- CC chloromercuribenzoic acid. Slightly activated by Mg(2+) and Ca(2+). CC Unaffected by Na(+), K(+), Ba(2+), EDTA, iodoacetic acid and N- CC ethylmalaimide. {ECO:0000269|PubMed:10635569}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.0. Stable between pH 5.0 and 8.0. CC {ECO:0000269|PubMed:10635569}; CC Temperature dependence: CC Optimum temperature is 37 degrees Celsius. Stable below 30 degrees CC Celsius. {ECO:0000269|PubMed:10635569}; CC -!- INDUCTION: By beta-1,3-xylan. {ECO:0000269|PubMed:10635569}. 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. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family. CC {ECO:0000255|PROSITE-ProRule:PRU01100}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB029043; BAA94698.1; -; Genomic_DNA. DR AlphaFoldDB; Q9LCB9; -. DR SMR; Q9LCB9; -. DR CAZy; CBM31; Carbohydrate-Binding Module Family 31. DR CAZy; GH26; Glycoside Hydrolase Family 26. DR KEGG; ag:BAA94698; -. DR BioCyc; MetaCyc:MONOMER-16528; -. DR BRENDA; 3.2.1.32; 6640. DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:InterPro. DR GO; GO:0030247; F:polysaccharide binding; ISS: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 Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing; KW Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation; Signal; KW Xylan degradation. FT SIGNAL 1..22 FT /evidence="ECO:0000269|PubMed:10635569, FT ECO:0000269|PubMed:10742274" FT CHAIN 23..460 FT /note="Beta-1,3-xylanase TXYA" FT /evidence="ECO:0000269|PubMed:10635569, FT ECO:0000269|PubMed:10742274" FT /id="PRO_0000403221" FT DOMAIN 23..337 FT /note="GH26" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01100" FT REGION 347..371 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 368..460 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 373..459 FT /evidence="ECO:0000250|UniProtKB:Q8RS40" FT DISULFID 404..409 FT /evidence="ECO:0000250|UniProtKB:Q8RS40" SQ SEQUENCE 460 AA; 51324 MW; 6EFA748496BA092A CRC64; MKKLAKMISV ATLGACAFQA HALDGKLVPD QGILVSVGQD VDSVNDYSSA MGTTPAGVTN YVGIVNLDGL STDADAGAGR NNIVELANQY PTSALIVGVS MNGEVQNVAN GQYNANIDTL IRTLGEFDRP VYLRWAYEVD GPWNGHNTED LKQSFRHVYQ RIRELGYADN ISMVWQVASY CPTAPGQLGT WWPGDDVVDW VGLSYFAPQD CNWDRVNEAA QWARSHNKPL FINESSPQRY QLADLTYSTD PAKGTNRQAK TDQQIWSEWF EPFFQFMVDN QDILKGFTYI NADWDSQWRW AAPYNEGYWG DSRVQVIPYI KQKWQETLSD PKFIRHSDEL FAQLGYGNSD GGNGGDNGGD NGGDNGGETP ENCTDDFNFN YVSDNEIEVY HVDKGWSAGW NYLCLDDYCL SGTKSNGAFS RSFSAQLGQT YKMTFKVEDI TGQGQQIIDK TVTFTNQVCN //