GUB_BACLI
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 25-MAY-2022, entry version 101.
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; Firmicutes; 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-beta-
RT 1,3-1,4-D-glucanase gene from Bacillus licheniformis. Predictive structural
RT 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 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; PTHR31062; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR PRINTS; PR00737; GLHYDRLASE16.
DR SUPFAM; SSF49899; SSF49899; 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
