ID XYNC_PAEBA Reviewed; 1086 AA. AC O69230; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 102. DE RecName: Full=Endo-1,4-beta-xylanase C; DE Short=Xylanase C; DE EC=3.2.1.8; DE AltName: Full=1,4-beta-D-xylan xylanohydrolase C; DE Flags: Precursor; GN Name=xynC; OS Paenibacillus barcinonensis. OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus. OX NCBI_TaxID=198119; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE RP SPECIFICITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23; RX PubMed=10463183; DOI=10.1099/13500872-145-8-2163; RA Blanco A., Diaz P., Zueco J., Parascandola P., Pastor F.I.J.; RT "A multidomain xylanase from a Bacillus sp. with a region homologous to RT thermostabilizing domains of thermophilic enzymes."; RL Microbiology 145:2163-2170(1999). CC -!- FUNCTION: Endoxylanase with high hydrolytic activity on birchwood and CC oat spelt xylan. Xylotetraose, xylotriose, xylobiose and xylose are the CC main products from birchwood xylan hydrolysis. Shows increasing CC activity on xylo-oligosaccharides of increasing length. Displays very CC low hydrolytic activity on Avicel, carboxymethylcellulose (CMC) and p- CC nitrophenyl-beta-xylopyranoside. Also shows transxylosidase activity, CC allowing the formation of xylo-oligosaccharides of higher degree of CC polymerization than the starting substrate. CC {ECO:0000269|PubMed:10463183}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; CC EC=3.2.1.8; Evidence={ECO:0000269|PubMed:10463183}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 5. Retains at least 50% of its maximum activity between CC pH 4.5 and 8.0. Is not active at pH values below 4.5, while at least CC 35% of maximum activity is found in the pH range 8.5-11.0. CC {ECO:0000269|PubMed:10463183}; CC Temperature dependence: CC Optimum temperature is 45 degrees Celsius. Is only stable at 55 CC degrees Celsius or lower temperatures. Retains more than 77% activity CC after 2 hours incubation at 55 degrees Celsius and pH 7. CC {ECO:0000269|PubMed:10463183}; CC -!- PATHWAY: Glycan degradation; xylan degradation. CC -!- DOMAIN: Consists of three different domains. The central region of the CC enzyme is the catalytic domain. The N-terminal region contains cenC- CC type cellulose-binding domains and seems to act as a thermostabilizing CC domain: a derivative lacking this region shows a lower optimum CC temperature for activity (35 degrees Celsius) than the full-length CC enzyme, and a reduced thermal stability that results in a complete CC inactivation of the enzyme after 2 hours incubation at 55 degrees CC Celsius. The C-terminal region contains family 9 carbohydrate-binding CC modules. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family. CC {ECO:0000305}. 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; AJ006645; CAA07173.1; -; Genomic_DNA. DR PIR; T17628; T17628. DR PDB; 4W8L; X-ray; 1.76 A; A/B/C=367-718. DR PDB; 4XUN; X-ray; 1.75 A; A/B/C=186-366. DR PDB; 4XUO; X-ray; 1.70 A; A/B=29-186. DR PDB; 4XUP; X-ray; 2.43 A; A/B/C/D/E/F=28-361. DR PDB; 4XUQ; X-ray; 1.95 A; A/B/C=186-366. DR PDB; 4XUR; X-ray; 1.67 A; A/B/C=186-366. DR PDB; 4XUT; X-ray; 1.80 A; A/B/C=186-366. DR PDBsum; 4W8L; -. DR PDBsum; 4XUN; -. DR PDBsum; 4XUO; -. DR PDBsum; 4XUP; -. DR PDBsum; 4XUQ; -. DR PDBsum; 4XUR; -. DR PDBsum; 4XUT; -. DR AlphaFoldDB; O69230; -. DR SMR; O69230; -. DR CAZy; CBM22; Carbohydrate-Binding Module Family 22. DR CAZy; CBM9; Carbohydrate-Binding Module Family 9. DR CAZy; GH10; Glycoside Hydrolase Family 10. DR UniPathway; UPA00114; -. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC. DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd00005; CBM9_like_1; 1. DR CDD; cd00241; DOMON_like; 1. DR Gene3D; 2.60.40.1190; -; 2. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR010502; Carb-bd_dom_fam9. DR InterPro; IPR003305; CenC_carb-bd. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR044846; GH10. DR InterPro; IPR031158; GH10_AS. DR InterPro; IPR001000; GH10_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1. DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1. DR Pfam; PF06452; CBM9_1; 2. DR Pfam; PF02018; CBM_4_9; 2. DR Pfam; PF00331; Glyco_hydro_10; 1. DR PRINTS; PR00134; GLHYDRLASE10. DR SMART; SM00633; Glyco_10; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF49344; CBD9-like; 2. DR SUPFAM; SSF49785; Galactose-binding domain-like; 2. DR PROSITE; PS00591; GH10_1; 1. DR PROSITE; PS51760; GH10_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase; KW Polysaccharide degradation; Repeat; Signal; Xylan degradation. FT SIGNAL 1..31 FT /evidence="ECO:0000255" FT CHAIN 32..1086 FT /note="Endo-1,4-beta-xylanase C" FT /id="PRO_0000371420" FT DOMAIN 35..183 FT /note="CBM-cenC 1" FT DOMAIN 197..359 FT /note="CBM-cenC 2" FT DOMAIN 365..710 FT /note="GH10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096" FT ACT_SITE 502 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 556 FT /evidence="ECO:0000250" FT ACT_SITE 620 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061" FT STRAND 37..41 FT /evidence="ECO:0007829|PDB:4XUO" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:4XUO" FT STRAND 52..56 FT /evidence="ECO:0007829|PDB:4XUO" FT STRAND 58..64 FT /evidence="ECO:0007829|PDB:4XUO" FT STRAND 67..70 FT /evidence="ECO:0007829|PDB:4XUO" FT STRAND 72..76 FT /evidence="ECO:0007829|PDB:4XUO" FT STRAND 84..88 FT /evidence="ECO:0007829|PDB:4XUO" FT TURN 90..92 FT /evidence="ECO:0007829|PDB:4XUO" FT STRAND 98..107 FT /evidence="ECO:0007829|PDB:4XUO" FT STRAND 114..123 FT /evidence="ECO:0007829|PDB:4XUO" FT STRAND 129..133 FT /evidence="ECO:0007829|PDB:4XUO" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:4XUO" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:4XUO" FT STRAND 146..152 FT /evidence="ECO:0007829|PDB:4XUO" FT STRAND 158..168 FT /evidence="ECO:0007829|PDB:4XUO" FT STRAND 173..184 FT /evidence="ECO:0007829|PDB:4XUO" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:4XUR" FT STRAND 216..218 FT /evidence="ECO:0007829|PDB:4XUR" FT STRAND 220..226 FT /evidence="ECO:0007829|PDB:4XUR" FT STRAND 229..238 FT /evidence="ECO:0007829|PDB:4XUR" FT STRAND 248..250 FT /evidence="ECO:0007829|PDB:4XUR" FT HELIX 252..254 FT /evidence="ECO:0007829|PDB:4XUR" FT STRAND 260..268 FT /evidence="ECO:0007829|PDB:4XUR" FT STRAND 271..286 FT /evidence="ECO:0007829|PDB:4XUR" FT STRAND 294..304 FT /evidence="ECO:0007829|PDB:4XUR" FT STRAND 309..316 FT /evidence="ECO:0007829|PDB:4XUR" FT HELIX 320..322 FT /evidence="ECO:0007829|PDB:4XUR" FT STRAND 324..332 FT /evidence="ECO:0007829|PDB:4XUR" FT HELIX 338..340 FT /evidence="ECO:0007829|PDB:4XUR" FT HELIX 344..346 FT /evidence="ECO:0007829|PDB:4XUR" FT STRAND 349..358 FT /evidence="ECO:0007829|PDB:4XUR" FT HELIX 371..375 FT /evidence="ECO:0007829|PDB:4W8L" FT STRAND 378..385 FT /evidence="ECO:0007829|PDB:4W8L" FT HELIX 387..390 FT /evidence="ECO:0007829|PDB:4W8L" FT HELIX 395..403 FT /evidence="ECO:0007829|PDB:4W8L" FT STRAND 405..411 FT /evidence="ECO:0007829|PDB:4W8L" FT HELIX 415..418 FT /evidence="ECO:0007829|PDB:4W8L" FT HELIX 428..439 FT /evidence="ECO:0007829|PDB:4W8L" FT STRAND 443..447 FT /evidence="ECO:0007829|PDB:4W8L" FT STRAND 452..454 FT /evidence="ECO:0007829|PDB:4W8L" FT HELIX 457..460 FT /evidence="ECO:0007829|PDB:4W8L" FT HELIX 472..490 FT /evidence="ECO:0007829|PDB:4W8L" FT TURN 491..493 FT /evidence="ECO:0007829|PDB:4W8L" FT STRAND 496..501 FT /evidence="ECO:0007829|PDB:4W8L" FT STRAND 508..510 FT /evidence="ECO:0007829|PDB:4W8L" FT HELIX 513..515 FT /evidence="ECO:0007829|PDB:4W8L" FT HELIX 519..523 FT /evidence="ECO:0007829|PDB:4W8L" FT HELIX 534..546 FT /evidence="ECO:0007829|PDB:4W8L" FT STRAND 551..558 FT /evidence="ECO:0007829|PDB:4W8L" FT TURN 559..561 FT /evidence="ECO:0007829|PDB:4W8L" FT HELIX 563..578 FT /evidence="ECO:0007829|PDB:4W8L" FT STRAND 585..588 FT /evidence="ECO:0007829|PDB:4W8L" FT STRAND 591..593 FT /evidence="ECO:0007829|PDB:4W8L" FT HELIX 599..610 FT /evidence="ECO:0007829|PDB:4W8L" FT TURN 611..613 FT /evidence="ECO:0007829|PDB:4W8L" FT STRAND 615..631 FT /evidence="ECO:0007829|PDB:4W8L" FT HELIX 638..659 FT /evidence="ECO:0007829|PDB:4W8L" FT TURN 660..662 FT /evidence="ECO:0007829|PDB:4W8L" FT STRAND 664..670 FT /evidence="ECO:0007829|PDB:4W8L" FT HELIX 674..676 FT /evidence="ECO:0007829|PDB:4W8L" FT HELIX 678..680 FT /evidence="ECO:0007829|PDB:4W8L" FT STRAND 682..684 FT /evidence="ECO:0007829|PDB:4W8L" FT STRAND 692..694 FT /evidence="ECO:0007829|PDB:4W8L" FT HELIX 702..708 FT /evidence="ECO:0007829|PDB:4W8L" FT HELIX 710..712 FT /evidence="ECO:0007829|PDB:4W8L" SQ SEQUENCE 1086 AA; 120586 MW; 4378361F1801A326 CRC64; MRGKWLRLCL AAVLIVSLLP GLGAGEWKAS AAKAGDILLS HSFEEGTTQG WTARGGVKVD VTAEQAYQGK QSLQTTGRTE AWNGPSLSLT DVVHKNEVVE ISGYVKLVAG SAPPDLKFTV ERRDRNGDTQ YDQVNAAEQV TDQKWVKLQG QYSYEQGSSL LLYLESTDAK AAYLLDEFQI RLVKAAPENP GEPGEAGQAL FKAYFEDGNI GNWRARGTEK LEVVSGIGHN SNRSLKTSSR SETYHGPLVE VLPYLQKGST VHISFWAMYD EGPATQVING SLEKEFNRDT ANLEYAMFAS TTLNKGQWKK IEADIIVPAE STGISGLRMY AETPWKQSSE VTETDTIPFY VDDVQITATE AIAIEKNIPD LAKKLGSSYA LGAAIDQTAL DPKDPHSELL TKHFNSITAG NFMKMDAMQP TEGKFVWSEA DKLVNFAAAN NMQVRGHTLL WHSQVPDWFF TDPNDPSKPA TREQLMQRMK THIQTIVSRY KGKVHTWDVV NEVISDGGGL RNQASGSKWR DIIGDVDGDG DDSDYIELAF RYAREADPDA VLVINDYGIE GSVSKMNDMV KLVEKLLAKG TPIDAIGFQM HVSMYGPDIK QIREAFNRAA ALGVHIQVTE LDMSIYSGNS EQEKPVTDEM MLEQAYRYRA LFDLFKEFDD RGVMDSVTLW GLADDGTWLD DFPVKGRKDA PLLFDRKLKA KPAYWALVDP STLPVYRNEW TASQAKVSLP DRKGQEDIIW GAVRALPFSH VIEGAVGTTG EVKTLWDGKQ LNLRIEVKDA TRLKGDQVEV FVSPEDMTAG KKNSTPKDGQ YIFNRDGGKG KDQKLYQVKE NKSGYVVYAS LPLSSADLAA GKVLSLDFRI TDKQPNGKTS IVVWNDVNNQ QPQKTENRGK LKLGFDLKHA KVMYGTPTVD GKEDKLWKKA VTITTDVKVT GNSGAKAKAK LLWDEKYLYV LAEVKDPLLS KKSANAHEQD SIELFIDLNK NQTNSYEEDD AQYRVNFDNE TSFGGSPRKE LFKSATRLTK EGYIVEAAIP LENVRTKESK WIGFDLQVND DGAGDGKRSS VFMWSDPSGN SYRDTSGFGS LLLMKK //