ID GUB_PAEMA Reviewed; 237 AA. AC P23904; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 2. DT 27-MAR-2024, entry version 116. DE RecName: Full=Beta-glucanase; DE EC=3.2.1.73; DE AltName: Full=1,3-1,4-beta-D-glucan 4-glucanohydrolase; DE AltName: Full=Endo-beta-1,3-1,4 glucanase; DE AltName: Full=Lichenase; DE Flags: Precursor; OS Paenibacillus macerans (Bacillus macerans). OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus. OX NCBI_TaxID=44252; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2274030; DOI=10.1007/bf00633829; RA Borriss R., Buettner K., Maentsaelae P.; RT "Structure of the beta-1,3-1,4-glucanase gene of Bacillus macerans: RT homologies to other beta-glucanases."; RL Mol. Gen. Genet. 222:278-283(1990). RN [2] RP ACTIVE SITE. RX PubMed=1360982; DOI=10.1016/s0021-9258(19)74005-8; RA Hoej P.B., Condron R., Traeger J.C., McAuliffe J.C., Stone B.A.; RT "Identification of glutamic acid 105 at the active site of Bacillus RT amyloliquefaciens 1,3-1,4-beta-D-glucan 4-glucanohydrolase using epoxide- RT based inhibitors."; RL J. Biol. Chem. 267:25059-25066(1992). RN [3] RP MUTAGENESIS OF GLU-128. RA Olsen O.; RL Thesis (1990), University of Aarhus, Denmark. RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=8099449; DOI=10.1073/pnas.90.11.5287; RA Keitel T., Simon O., Borriss R., Heinemann U.; RT "Molecular and active-site structure of a Bacillus 1,3-1,4-beta- RT glucanase."; RL Proc. Natl. Acad. Sci. U.S.A. 90:5287-5291(1993). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). RX PubMed=7588726; DOI=10.1111/j.1432-1033.1995.tb20883.x; RA Hahn M., Keitel T., Heinemann U.; RT "Crystal and molecular structure at 0.16-nm resolution of the hybrid RT Bacillus endo-1,3-1,4-beta-D-glucan 4-glucanohydrolase H(A16-M)."; RL Eur. J. Biochem. 232:849-858(1995). CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D- CC glucans containing (1->3)- and (1->4)-bonds.; EC=3.2.1.73; CC -!- MISCELLANEOUS: Beta-glucanases of Bacillus have a substrate range CC similar to lichenase of germinating barley. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {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; X55959; CAA39426.1; -; Genomic_DNA. DR PIR; S11927; S11927. DR PDB; 1AJK; X-ray; 1.80 A; A/B=107-237. DR PDB; 1AJO; X-ray; 2.07 A; A/B=37-149. DR PDB; 1AXK; X-ray; 2.10 A; A/B=82-237. DR PDB; 1BYH; X-ray; 2.80 A; A=40-237. DR PDB; 1CPM; X-ray; 2.00 A; A=82-237. DR PDB; 1CPN; X-ray; 1.80 A; A=82-237. DR PDB; 1GLH; X-ray; 2.00 A; A=37-237. DR PDB; 1MAC; X-ray; 2.30 A; A/B=26-237. DR PDB; 1U0A; X-ray; 1.64 A; A/B/C/D=37-237. DR PDB; 2AYH; X-ray; 1.60 A; A=37-237. DR PDBsum; 1AJK; -. DR PDBsum; 1AJO; -. DR PDBsum; 1AXK; -. DR PDBsum; 1BYH; -. DR PDBsum; 1CPM; -. DR PDBsum; 1CPN; -. DR PDBsum; 1GLH; -. DR PDBsum; 1MAC; -. DR PDBsum; 1U0A; -. DR PDBsum; 2AYH; -. DR AlphaFoldDB; P23904; -. DR SMR; P23904; -. DR STRING; 44252.DJ90_6408; -. DR DrugBank; DB02379; Beta-D-Glucose. DR CAZy; GH16; Glycoside Hydrolase Family 16. DR EvolutionaryTrace; P23904; -. DR GO; GO:0042972; F:licheninase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd02175; GH16_lichenase; 1. DR Gene3D; 2.60.120.200; -; 1. DR InterPro; IPR044791; Beta-glucanase/XTH. DR InterPro; IPR008264; Beta_glucanase. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR000757; GH16. DR InterPro; IPR008263; GH16_AS. DR PANTHER; PTHR31062; XYLOGLUCAN ENDOTRANSGLUCOSYLASE/HYDROLASE PROTEIN 8-RELATED; 1. DR PANTHER; PTHR31062:SF185; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE PROTEIN 6-RELATED; 1. DR Pfam; PF00722; Glyco_hydro_16; 1. DR PRINTS; PR00737; GLHYDRLASE16. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS01034; GH16_1; 1. DR PROSITE; PS51762; GH16_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Glycosidase; Hydrolase; Signal. FT SIGNAL 1..23 FT /evidence="ECO:0000255" FT CHAIN 24..237 FT /note="Beta-glucanase" FT /id="PRO_0000011789" FT DOMAIN 28..237 FT /note="GH16" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098" FT ACT_SITE 128 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064" FT ACT_SITE 132 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064" FT DISULFID 55..84 FT /evidence="ECO:0000269|PubMed:8099449" FT MUTAGEN 128 FT /note="E->D,N,A,L,P,R,H,C,S,Y: Loss of activity." FT /evidence="ECO:0000269|Ref.3" FT STRAND 15..24 FT /evidence="ECO:0007829|PDB:1AJO" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:2AYH" FT STRAND 38..43 FT /evidence="ECO:0007829|PDB:2AYH" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:1GLH" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:2AYH" FT HELIX 59..61 FT /evidence="ECO:0007829|PDB:2AYH" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:2AYH" FT STRAND 70..78 FT /evidence="ECO:0007829|PDB:2AYH" FT STRAND 81..91 FT /evidence="ECO:0007829|PDB:2AYH" FT STRAND 95..103 FT /evidence="ECO:0007829|PDB:2AYH" FT STRAND 110..118 FT /evidence="ECO:0007829|PDB:2AYH" FT HELIX 120..122 FT /evidence="ECO:0007829|PDB:2AYH" FT STRAND 127..134 FT /evidence="ECO:0007829|PDB:2AYH" FT HELIX 135..137 FT /evidence="ECO:0007829|PDB:1CPM" FT STRAND 140..147 FT /evidence="ECO:0007829|PDB:2AYH" FT STRAND 155..158 FT /evidence="ECO:0007829|PDB:2AYH" FT HELIX 163..165 FT /evidence="ECO:0007829|PDB:2AYH" FT STRAND 168..175 FT /evidence="ECO:0007829|PDB:2AYH" FT STRAND 178..183 FT /evidence="ECO:0007829|PDB:2AYH" FT STRAND 186..191 FT /evidence="ECO:0007829|PDB:2AYH" FT STRAND 200..211 FT /evidence="ECO:0007829|PDB:2AYH" FT HELIX 213..216 FT /evidence="ECO:0007829|PDB:2AYH" FT STRAND 225..236 FT /evidence="ECO:0007829|PDB:2AYH" SQ SEQUENCE 237 AA; 26589 MW; 436EABCDFFC87781 CRC64; MKKKSCFTLV TTFAFSLIFS VSALAGSVFW EPLSYFNRST WEKADGYSNG GVFNCTWRAN NVNFTNDGKL KLGLTSSAYN KFDCAEYRST NIYGYGLYEV SMKPAKNTGI VSSFFTYTGP AHGTQWDEID IEFLGKDTTK VQFNYYTNGV GGHEKVISLG FDASKGFHTY AFDWQPGYIK WYVDGVLKHT ATANIPSTPG KIMMNLWNGT GVDDWLGSYN GANPLYAEYD WVKYTSN //