GUB_PAEMA
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 25-MAY-2022, entry version 112.
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; Firmicutes; 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}.
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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 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..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
