ID   GUB_RHOMR               Reviewed;         286 AA.
AC   P45798;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 79.
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   Rhodothermus marinus (Rhodothermus obamensis).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Rhodothermus.
OX   NCBI_TaxID=29549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=21 / ITI-378;
RX   PubMed=7925416; DOI=10.1111/j.1432-1033.1994.00923.x;
RA   Spilliaert R., Hreggvidsson G.O., Kristjansson J.K., Eggertsson G.,
RA   Palsdottir A.;
RT   "Cloning and sequencing of a Rhodothermus marinus gene, bglA, coding for a
RT   thermostable beta-glucanase and its expression in Escherichia coli.";
RL   Eur. J. Biochem. 224:923-930(1994).
CC   -!- FUNCTION: Shows activity on lichenan, beta-glucan and laminarin but not
CC       on CMC cellulose or xylan.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0.;
CC       Temperature dependence:
CC         Optimum temperature is 85 degrees Celsius.;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR   EMBL; U04836; AAA60459.1; -; Genomic_DNA.
DR   PIR; S48201; S48201.
DR   AlphaFoldDB; P45798; -.
DR   SMR; P45798; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   BRENDA; 3.2.1.73; 5425.
DR   GO; GO:0042972; F:licheninase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR008263; GH16_AS.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS01034; GH16_1; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   1: Evidence at protein level;
KW   Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..286
FT                   /note="Beta-glucanase"
FT                   /id="PRO_0000011794"
FT   DOMAIN          48..286
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   ACT_SITE        158
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT   ACT_SITE        163
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
SQ   SEQUENCE   286 AA;  33145 MW;  7215C33624135191 CRC64;
     MCTMPLMKLK KMMRRTAFLL SVLIGCSMLG SDRSDKAPHW ELVWSDEFDY SGLPDPEKWD
     YDVGGHGWGN QELQYYTRAR IENARVGGGV LIIEARHEPY EGREYTSARL VTRGKASWTY
     GRFEIRARLP SGRGTWPAIW MLPDRQTYGS AYWPDNGEID IMEHVGFNPD VVHGTVHTKA
     YNHLLGTQRG GSIRVPTART DFHVYAIEWT PEEIRWFVDD SLYYRFPNER LTDPEADWRH
     WPFDQPFHLI MNIAVGGAWG GQQGVDPEAF PAQLVVDYVR VYRWVE