GUB_BACAM
ID GUB_BACAM Reviewed; 239 AA.
AC P07980;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=bglA;
OS Bacillus amyloliquefaciens (Bacillus velezensis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=1390;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BE 20/78;
RX PubMed=3106158; DOI=10.1016/0378-1119(86)90278-7;
RA Hofemeister J., Kurtz A., Borriss R., Knowles J.;
RT "The beta-glucanase gene from Bacillus amyloliquefaciens shows extensive
RT homology with that of Bacillus subtilis.";
RL Gene 49:177-187(1986).
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; M15674; AAA87323.1; -; Genomic_DNA.
DR PIR; A29091; A29091.
DR AlphaFoldDB; P07980; -.
DR SMR; P07980; -.
DR STRING; 692420.BAMF_3732; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR eggNOG; COG2273; Bacteria.
DR BRENDA; 3.2.1.73; 630.
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 3: Inferred from homology;
KW Disulfide bond; Glycosidase; Hydrolase; Signal.
FT SIGNAL 1..25
FT CHAIN 26..239
FT /note="Beta-glucanase"
FT /id="PRO_0000011786"
FT DOMAIN 26..239
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 134
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT DISULFID 57..86
FT /evidence="ECO:0000250"
SQ SEQUENCE 239 AA; 26928 MW; A76A64268A7AAA0B CRC64;
MKRVLLILVT GLFMSLCGIT SSVSAQTGGS FFEPFNSYNS GLWQKADGYS NGDMFNCTWR
ANNVSMTSLG EMRLALTSPS YNKFDCGENR SVQTYGYGLY EVRMKPAKNT GIVSSFFTYT
GPTEGTPWDE IDIEFLGKDT TKVQFNYYTN GAGNHEKFAD LGFDAANAYH TYAFDWQPNS
IKWYVDGQLK HTATTQIPAA PGKIMMNLWN GTGVDDWLGS YNGVNPIYAH YDWMRYRKK