GUB_ACETH
ID GUB_ACETH Reviewed; 334 AA.
AC Q84C00; P29716; P37074;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=Laminarinase;
DE AltName: Full=Lichenase;
DE Flags: Precursor;
GN Name=licB; Synonyms=lam1;
OS Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium
OS thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=1515;
RN [1]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=F7;
RX PubMed=1755832; DOI=10.1016/0006-291x(91)91217-z;
RA Zverlov V.V., Laptev D.A., Tishkov V.I., Velikodvorskaja G.A.;
RT "Nucleotide sequence of the Clostridium thermocellum laminarinase gene.";
RL Biochem. Biophys. Res. Commun. 181:507-512(1991).
RN [2]
RP SEQUENCE REVISION.
RA Zverlov V.V.;
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lv W.-P., Xu Z.-R., Li W.-F., Sun J.-Y., Xu Y.-X., Gu S.-H.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP CHARACTERIZATION.
RC STRAIN=F7;
RA Zverlov V.V., Velikodvorskaja G.A.;
RT "Cloning the Clostridium thermocellum thermostable laminarinase gene in
RT Escherichia coli; the properties of the enzyme thus produced.";
RL Biotechnol. Lett. 12:811-816(1990).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR EMBL; X58392; CAA41281.1; -; Genomic_DNA.
DR EMBL; AY225318; AAO74890.1; -; Genomic_DNA.
DR PIR; JS0611; JS0611.
DR AlphaFoldDB; Q84C00; -.
DR SMR; Q84C00; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR BRENDA; 3.2.1.73; 1530.
DR GO; GO:0042972; F:licheninase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR Gene3D; 1.10.1330.10; -; 1.
DR InterPro; IPR044791; Beta-glucanase/XTH.
DR InterPro; IPR008264; Beta_glucanase.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR008263; GH16_AS.
DR PANTHER; PTHR31062; PTHR31062; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR PRINTS; PR00737; GLHYDRLASE16.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF63446; SSF63446; 1.
DR PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 2.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..334
FT /note="Beta-glucanase"
FT /id="PRO_0000011792"
FT DOMAIN 28..248
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT DOMAIN 267..334
FT /note="Dockerin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT REGION 246..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..263
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 140
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT CONFLICT 97
FT /note="S -> T (in Ref. 1; CAA41281 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="A -> V (in Ref. 1; CAA41281 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="E -> G (in Ref. 1; CAA41281 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="K -> I (in Ref. 1; CAA41281 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 304..334
FT /note="QSVADVNRDGRIDSTDLTMLKRYLIRAIPSL -> PQDGCGRHDRVVDSGSK
FT (in Ref. 1; CAA41281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 37942 MW; 3079DEF1CEE5A664 CRC64;
MKNRVISLLM ASLLLVLSVI VAPFYKAEAA TVVNTPFVAV FSNFDSSQWE KADWANGSVF
NCVWKPSQVT FSNGKMILTL DREYGGSYPY KSGEYRSKSF FGYGYYEVRM KAAKNVGIVS
SFFTYTGPSD NNPWDEIDIE FLGKDTTKAQ FNWYKNEVGG NEYLHNLGFD ASQDFHTYGF
EWRPDYIDFY VDGKKVYRGT RNIPVTPGKI MMNLWPGKGV DEWLGRYDGR TPLQAEYEYV
KYYPNGVPQD NPTPTPTIAP STPTNPNLPL KGDVNGDGHV NSSDYSLFKR YLLRVIDRFP
VGDQSVADVN RDGRIDSTDL TMLKRYLIRA IPSL
