GUB_ACET2
ID GUB_ACET2 Reviewed; 334 AA.
AC A3DBX3; P29716; P37074;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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; OrderedLocusNames=Cthe_0211;
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1740123; DOI=10.1111/j.1432-1033.1992.tb16600.x;
RA Schimming S., Schwarz W.H., Staudenbauer W.L.;
RT "Structure of the Clostridium thermocellum gene licB and the encoded beta-
RT 1,3-1,4-glucanase. A catalytic region homologous to Bacillus lichenases
RT joined to the reiterated domain of clostridial cellulases.";
RL Eur. J. Biochem. 204:13-19(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: May form part of a multienzyme complex (cellulosome).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR EMBL; X63355; CAA44959.1; -; Genomic_DNA.
DR EMBL; CP000568; ABN51452.1; -; Genomic_DNA.
DR PIR; S23498; S23498.
DR RefSeq; WP_003512300.1; NC_009012.1.
DR PDB; 3WVJ; X-ray; 1.95 A; A/B=30-249.
DR PDBsum; 3WVJ; -.
DR AlphaFoldDB; A3DBX3; -.
DR SMR; A3DBX3; -.
DR STRING; 203119.Cthe_0211; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR EnsemblBacteria; ABN51452; ABN51452; Cthe_0211.
DR KEGG; cth:Cthe_0211; -.
DR eggNOG; COG2273; Bacteria.
DR HOGENOM; CLU_071026_1_0_9; -.
DR OMA; WYVSDGW; -.
DR OrthoDB; 1046649at2; -.
DR BioCyc; MetaCyc:MON-16465; -.
DR BRENDA; 3.2.1.73; 1530.
DR Proteomes; UP000002145; Chromosome.
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 3D-structure; Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..334
FT /note="Beta-glucanase"
FT /id="PRO_0000284719"
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 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 STRAND 37..40
FT /evidence="ECO:0007829|PDB:3WVJ"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:3WVJ"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3WVJ"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:3WVJ"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:3WVJ"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:3WVJ"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:3WVJ"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:3WVJ"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:3WVJ"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:3WVJ"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:3WVJ"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:3WVJ"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:3WVJ"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:3WVJ"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:3WVJ"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:3WVJ"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:3WVJ"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:3WVJ"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:3WVJ"
FT STRAND 208..219
FT /evidence="ECO:0007829|PDB:3WVJ"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:3WVJ"
FT STRAND 233..245
FT /evidence="ECO:0007829|PDB:3WVJ"
SQ SEQUENCE 334 AA; 37897 MW; 0837564E9726F281 CRC64;
MKNRVISLLM ASLLLVLSVI VAPFYKAEAA TVVNTPFVAV FSNFDSSQWE KADWANGSVF
NCVWKPSQVT FSNGKMILTL DREYGGSYPY KSGEYRTKSF FGYGYYEVRM KAAKNVGIVS
SFFTYTGPSD NNPWDEIDIE FLGKDTTKVQ FNWYKNGVGG NEYLHNLGFD ASQDFHTYGF
EWRPDYIDFY VDGKKVYRGT RNIPVTPGKI MMNLWPGIGV DEWLGRYDGR TPLQAEYEYV
KYYPNGVPQD NPTPTPTIAP STPTNPNLPL KGDVNGDGHV NSSDYSLFKR YLLRVIDRFP
VGDQSVADVN RDGRIDSTDL TMLKRYLIRA IPSL
