ID 3XYN1_VIBSX Reviewed; 576 AA. AC D5MP61; DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot. DT 13-JUL-2010, sequence version 1. DT 04-NOV-2026, entry version 42. DE RecName: Full=Beta-1,3-xylanase XYL4 {ECO:0000303|PubMed:19605459}; DE EC=3.2.1.32; DE AltName: Full=Beta-1,3-xylanase {ECO:0000312|EMBL:BAD51934.1}; DE Flags: Precursor; GN Name=xyl4 {ECO:0000312|EMBL:BAD51934.1}; OS Vibrio sp. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=678; RN [1] {ECO:0000305, ECO:0000312|EMBL:BAD51934.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLU-138; RP GLU-234 AND GLU-268. RC STRAIN=AX-4 {ECO:0000312|EMBL:BAD51934.1}; RX PubMed=15743273; DOI=10.1042/bj20050190; RA Kiyohara M., Sakaguchi K., Yamaguchi K., Araki T., Nakamura T., Ito M.; RT "Molecular cloning and characterization of a novel beta-1,3-xylanase RT possessing two putative carbohydrate-binding modules from a marine RT bacterium Vibrio sp. strain AX-4."; RL Biochem. J. 388:949-957(2005). RN [2] {ECO:0000305} RP CBM31 DOMAIN. RC STRAIN=AX-4 {ECO:0000269|PubMed:19605459}; RX PubMed=19605459; DOI=10.1093/jb/mvp108; RA Kiyohara M., Sakaguchi K., Yamaguchi K., Araki T., Ito M.; RT "Characterization and application of carbohydrate-binding modules of beta- RT 1,3-xylanase XYL4."; RL J. Biochem. 146:633-641(2009). RN [3] {ECO:0000305} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH MAGNESIUM. RC STRAIN=AX-4 {ECO:0000269|Ref.3}; RA Sakaguchi K., Kawamura T., Watanabe N., Kiyohara M., Yamaguchi K., Ito M., RA Tanaka I.; RT "Atomic resolution analysis of beta-1,3-xylanase catalytic module from RT Vibrio sp. AX-4."; RL Submitted (FEB-2006) to the PDB data bank. CC -!- FUNCTION: Catalyzes the hydrolysis of beta-1,3-xylan into CC oligosaccharides, mainly xylobiose, xylotriose and xylotetraose. CC Converts beta-1,3-xylotriose into xylose and xylobiose, converts beta- CC 1,3-xylotetraose mainly into xylotriose and xylose, converts beta-1,3- CC xylopentaose into xylobiose and xylotriose. Does not hydrolyze CC beta-1,4-xylan, beta-1,4-mannan, beta-1,4-glucan, beta-1,3-xylobiose or CC p-nitrophenyl-beta-xyloside. {ECO:0000269|PubMed:15743273}. 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:15743273}; CC -!- ACTIVITY REGULATION: Completely inhibited by Hg(2+), partially CC inhibited by Mn(2+), Cu(2+) and Pb(2+). Unaffected by Ca(2+), Mg(2+) CC and EDTA. {ECO:0000269|PubMed:15743273}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=7.4 mM for beta-1,3-xylotetraose {ECO:0000269|PubMed:15743273}; CC KM=7.5 mM for beta-1,3-xylopentaose {ECO:0000269|PubMed:15743273}; CC pH dependence: CC Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:15743273}; CC Temperature dependence: CC Optimum temperature is 37 degrees Celsius. Inactive above 60 degrees CC Celsius. {ECO:0000269|PubMed:15743273}; CC -!- DOMAIN: The carbohydrate binding modules (CBM) bind 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, ECO:0000269|PubMed:15743273}. 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; AB121027; BAD51934.1; -; Genomic_DNA. DR PDB; 2DDX; X-ray; 0.86 A; A=23-349. DR PDB; 3VPL; X-ray; 1.20 A; A=23-349. DR AlphaFoldDB; D5MP61; -. DR MDposit; D5MP61; -. DR SMR; D5MP61; -. DR CAZy; CBM31; Carbohydrate-Binding Module Family 31. DR CAZy; GH26; Glycoside Hydrolase Family 26. DR BRENDA; 3.2.1.32; 6640. DR EvolutionaryTrace; D5MP61; -. 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:0033905; F:xylan endo-1,3-beta-xylosidase activity; IDA:UniProtKB. DR GO; GO:0006080; P:substituted mannan metabolic process; IEA:InterPro. DR GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB. DR FunFam; 3.20.20.80:FF:000335; Beta-1,3-xylanase TXYA; 1. DR Gene3D; 2.60.40.2450; Beta-1,3-xylanase, CBM31 domain; 2. 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; IPR017853; GH_hydrolase_sf. DR InterPro; IPR000805; Glyco_hydro_26. 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; 2. 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 Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation; Repeat; KW Signal; Xylan degradation. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..576 FT /note="Beta-1,3-xylanase XYL4" FT /evidence="ECO:0000255" FT /id="PRO_0000403220" FT DOMAIN 23..293 FT /note="GH26" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01100" FT REGION 347..367 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 363..453 FT /note="Carbohydrate binding module (CBM) 1" FT REGION 450..486 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 487..574 FT /note="Carbohydrate binding module (CBM) 2" FT COMPBIAS 347..360 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 456..485 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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 368..452 FT /evidence="ECO:0000250|UniProtKB:Q8RS40" FT DISULFID 399..404 FT /evidence="ECO:0000250|UniProtKB:Q8RS40" FT DISULFID 490..574 FT /evidence="ECO:0000250|UniProtKB:Q8RS40" FT DISULFID 521..526 FT /evidence="ECO:0000250|UniProtKB:Q8RS40" FT MUTAGEN 138 FT /note="E->D: Very low catalytic activity." FT /evidence="ECO:0000269|PubMed:15743273" FT MUTAGEN 138 FT /note="E->Q: Complete loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:15743273" FT MUTAGEN 234 FT /note="E->D: Very low catalytic activity." FT /evidence="ECO:0000269|PubMed:15743273" FT MUTAGEN 234 FT /note="E->Q: Complete loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:15743273" FT MUTAGEN 268 FT /note="E->Q: Catalytic activity reduced by 30%." FT /evidence="ECO:0000269|PubMed:15743273" FT TURN 24..27 FT /evidence="ECO:0007829|PDB:2DDX" FT STRAND 30..40 FT /evidence="ECO:0007829|PDB:2DDX" FT HELIX 41..51 FT /evidence="ECO:0007829|PDB:2DDX" FT STRAND 56..63 FT /evidence="ECO:0007829|PDB:2DDX" FT TURN 64..66 FT /evidence="ECO:0007829|PDB:2DDX" FT STRAND 70..72 FT /evidence="ECO:0007829|PDB:2DDX" FT STRAND 74..78 FT /evidence="ECO:0007829|PDB:2DDX" FT HELIX 83..89 FT /evidence="ECO:0007829|PDB:2DDX" FT STRAND 93..100 FT /evidence="ECO:0007829|PDB:2DDX" FT HELIX 105..109 FT /evidence="ECO:0007829|PDB:2DDX" FT TURN 110..113 FT /evidence="ECO:0007829|PDB:2DDX" FT HELIX 114..125 FT /evidence="ECO:0007829|PDB:2DDX" FT STRAND 131..135 FT /evidence="ECO:0007829|PDB:2DDX" FT HELIX 142..144 FT /evidence="ECO:0007829|PDB:2DDX" FT HELIX 148..165 FT /evidence="ECO:0007829|PDB:2DDX" FT TURN 168..170 FT /evidence="ECO:0007829|PDB:2DDX" FT STRAND 171..176 FT /evidence="ECO:0007829|PDB:2DDX" FT HELIX 189..191 FT /evidence="ECO:0007829|PDB:2DDX" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:2DDX" FT STRAND 199..207 FT /evidence="ECO:0007829|PDB:2DDX" FT HELIX 208..211 FT /evidence="ECO:0007829|PDB:2DDX" FT HELIX 214..226 FT /evidence="ECO:0007829|PDB:2DDX" FT STRAND 230..235 FT /evidence="ECO:0007829|PDB:2DDX" FT TURN 242..245 FT /evidence="ECO:0007829|PDB:2DDX" FT TURN 251..253 FT /evidence="ECO:0007829|PDB:2DDX" FT HELIX 262..265 FT /evidence="ECO:0007829|PDB:2DDX" FT HELIX 266..270 FT /evidence="ECO:0007829|PDB:2DDX" FT HELIX 271..279 FT /evidence="ECO:0007829|PDB:2DDX" FT TURN 280..283 FT /evidence="ECO:0007829|PDB:2DDX" FT STRAND 284..290 FT /evidence="ECO:0007829|PDB:2DDX" FT HELIX 294..296 FT /evidence="ECO:0007829|PDB:2DDX" FT HELIX 298..300 FT /evidence="ECO:0007829|PDB:2DDX" FT TURN 302..306 FT /evidence="ECO:0007829|PDB:2DDX" FT HELIX 314..316 FT /evidence="ECO:0007829|PDB:2DDX" FT HELIX 318..328 FT /evidence="ECO:0007829|PDB:2DDX" FT HELIX 340..343 FT /evidence="ECO:0007829|PDB:2DDX" SQ SEQUENCE 576 AA; 62591 MW; E04449C5F703884D CRC64; MKRTYLSLIA AGVMSLSVSA WSLDGVLVPE SGILVSVGQD VDSVNDYASA LGTIPAGVTN YVGIVNLDGL NSDADAGAGR NNIAELANAY PTSALVVGVS MNGEVDAVAS GRYNANIDTL LNTLAGYDRP VYLRWAYEVD GPWNGHSPSG IVTSFQYVHD RIIALGHQAK ISLVWQVASY CPTPGGQLDQ WWPGSEYVDW VGLSYFAPQD CNWDRVNEAA QFARSKGKPL FLNESTPQRY QVADLTYSAD PAKGTNRQSK TSQQLWDEWF APYFQFMSDN SDIVKGFTYI NADWDSQWRW AAPYNEGYWG DSRVQANALI KSNWQQEIAK GQYINHSETL FETLGYGSTG GGDNGGGDNG GTNPPEPCNE EFGYRYVSDS TIEVFHKNNG WSAEWNYVCL NGLCLQGEIK NGEYVKQFDA QLGSTYGIEF KVADGESQFI TDKSVTFENK QCGSTGTPGG GDNGSGGDNG GDNGSGGDNG SGGGTDPSQC SADFGYNYRS DTEIEVFHKD LGWSASWNYI CLDDYCVPGD KSGDSYNRSF NATLGSDYKI TFKVEDSASQ FITEKNITFV NTSCAQ //