3XYN2_VIBSX
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 03-AUG-2022, entry version 67.
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; Proteobacteria; 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}.
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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:MON-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; -; 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 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
