ID GUB_BACLI Reviewed; 243 AA. AC P27051; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 27-MAR-2024, entry version 105. 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; GN Name=bg1; OS Bacillus licheniformis. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1402; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2026156; DOI=10.1111/j.1432-1033.1991.tb15916.x; RA Lloberas J., Perez-Pons J.A., Querol E.; RT "Molecular cloning, expression and nucleotide sequence of the endo- RT beta-1,3-1,4-D-glucanase gene from Bacillus licheniformis. Predictive RT structural analyses of the encoded polypeptide."; RL Eur. J. Biochem. 197:337-343(1991). RN [2] RP SEQUENCE REVISION. RA Querol E.; RL Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP MUTAGENESIS. RX PubMed=1354172; DOI=10.1016/0014-5793(92)81262-k; RA Planas A., Juncosa M., Lloberas J., Querol E.; RT "Essential catalytic role of Glu134 in endo-beta-1,3-1,4-D-glucan 4- RT glucanohydrolase from B. licheniformis as determined by site-directed RT mutagenesis."; RL FEBS Lett. 308:141-145(1992). RN [4] RP MUTAGENESIS. RX PubMed=8182059; DOI=10.1016/s0021-9258(17)36655-3; RA Juncosa M., Pons J., Dot T., Querol E., Planas A.; RT "Identification of active site carboxylic residues in Bacillus RT licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase by site-directed RT mutagenesis."; RL J. Biol. Chem. 269:14530-14535(1994). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND DISULFIDE BOND. RX PubMed=7589539; DOI=10.1016/0014-5793(95)01111-q; RA Hahn M., Pons J., Planas A., Querol E., Heinemann U.; RT "Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4- RT glucanohydrolase at 1.8-A resolution."; RL FEBS Lett. 374:221-224(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; X57279; CAA40547.1; -; Genomic_DNA. DR PIR; S15388; S15388. DR PDB; 1GBG; X-ray; 1.80 A; A=30-243. DR PDB; 3D6E; X-ray; 2.40 A; A/B=30-243. DR PDBsum; 1GBG; -. DR PDBsum; 3D6E; -. DR AlphaFoldDB; P27051; -. DR SMR; P27051; -. DR CAZy; GH16; Glycoside Hydrolase Family 16. DR BRENDA; 3.2.1.73; 669. DR SABIO-RK; P27051; -. DR EvolutionaryTrace; P27051; -. 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..27 FT /evidence="ECO:0000255" FT CHAIN 28..243 FT /note="Beta-glucanase" FT /id="PRO_0000011788" FT DOMAIN 29..243 FT /note="GH16" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098" FT ACT_SITE 134 FT /note="Nucleophile" FT ACT_SITE 138 FT /note="Proton donor" FT DISULFID 61..90 FT /evidence="ECO:0000269|PubMed:7589539" FT MUTAGEN 51 FT /note="D->N: 30% of wild-type activity." FT MUTAGEN 89 FT /note="D->N: 85% of wild-type activity." FT MUTAGEN 92 FT /note="E->Q: 3% of wild-type activity." FT MUTAGEN 105 FT /note="E->Q: 50% of wild-type activity." FT MUTAGEN 133 FT /note="D->N: 15% of wild-type activity." FT MUTAGEN 134 FT /note="E->Q: 0.2% of wild-type activity." FT MUTAGEN 136 FT /note="D->N: 0.5% of wild-type activity." FT MUTAGEN 138 FT /note="E->Q: Complete loss of activity." FT MUTAGEN 143 FT /note="D->N: 65% of wild-type activity." FT MUTAGEN 160 FT /note="E->Q: 15% of wild-type activity." FT MUTAGEN 168 FT /note="D->N: 60% of wild-type activity." FT MUTAGEN 179 FT /note="D->N: 80% of wild-type activity." FT MUTAGEN 190 FT /note="D->N: 70% of wild-type activity." FT MUTAGEN 219 FT /note="D->N: No change in activity." FT CONFLICT 232 FT /note="S -> Y (in Ref. 5)" FT /evidence="ECO:0000305" FT STRAND 35..37 FT /evidence="ECO:0007829|PDB:1GBG" FT TURN 44..46 FT /evidence="ECO:0007829|PDB:1GBG" FT STRAND 47..49 FT /evidence="ECO:0007829|PDB:1GBG" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:1GBG" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:1GBG" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:1GBG" FT STRAND 76..84 FT /evidence="ECO:0007829|PDB:1GBG" FT STRAND 87..97 FT /evidence="ECO:0007829|PDB:1GBG" FT STRAND 101..109 FT /evidence="ECO:0007829|PDB:1GBG" FT STRAND 116..124 FT /evidence="ECO:0007829|PDB:1GBG" FT HELIX 126..128 FT /evidence="ECO:0007829|PDB:1GBG" FT STRAND 133..140 FT /evidence="ECO:0007829|PDB:1GBG" FT STRAND 146..153 FT /evidence="ECO:0007829|PDB:1GBG" FT STRAND 161..164 FT /evidence="ECO:0007829|PDB:1GBG" FT TURN 169..171 FT /evidence="ECO:0007829|PDB:1GBG" FT STRAND 174..181 FT /evidence="ECO:0007829|PDB:1GBG" FT STRAND 184..189 FT /evidence="ECO:0007829|PDB:1GBG" FT STRAND 192..197 FT /evidence="ECO:0007829|PDB:1GBG" FT STRAND 206..217 FT /evidence="ECO:0007829|PDB:1GBG" FT HELIX 219..222 FT /evidence="ECO:0007829|PDB:1GBG" FT STRAND 231..242 FT /evidence="ECO:0007829|PDB:1GBG" SQ SEQUENCE 243 AA; 27435 MW; 651188D9AAD609A5 CRC64; MSYRVKRMLM LLVTGLFLSL STFAASASAQ TGGSFYEPFN NYNTGLWQKA DGYSNGNMFN CTWRANNVSM TSLGEMRLSL TSPSYNKFDC GENRSVQTYG YGLYEVNMKP AKNVGIVSSF FTYTGPTDGT PWDEIDIEFL GKDTTKVQFN YYTNGVGNHE KIVNLGFDAA NSYHTYAFDW QPNSIKWYVD GQLKHTATTQ IPQTPGKIMM NLWNGAGVDE WLGSYNGVTP LSRSLHWVRY TKR //