A3DBX3 (GUB_CLOTH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-glucanase
EC=3.2.1.73

Alternative name(s):
1,3-1,4-beta-D-glucan 4-glucanohydrolase
Endo-beta-1,3-1,4 glucanase
Laminarinase
Lichenase

Gene names

Name:	licB
Synonyms:	lam1
Ordered Locus Names:	Cthe_0211

Organism

Clostridium thermocellum (strain ATCC 27405 / DSM 1237) [Complete proteome] [HAMAP]

Taxonomic identifier

203119 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › Clostridium thermocellum

Protein attributes

Sequence length	334 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.
Subunit structure	May form part of a multienzyme complex (cellulosome) By similarity.
Domain	A 24 residue domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 16 family.

Ontologies

Keywords
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	polysaccharide catabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	licheninase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Potential
	Chain	28 – 334	307	Beta-glucanase		PRO_0000284719
Regions
	Repeat	273 – 296	24	1
	Repeat	308 – 331	24	2
	Region	273 – 331	59	2 X 24 AA approximate repeats
	Compositional bias	252 – 269	18	Pro/Thr-rich (linker)
Sites
	Active site	136	1	Nucleophile By similarity
	Active site	140	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	A3DBX3 [UniParc]. Last modified March 20, 2007. Version 1. Checksum: 0837564E9726F281	FASTA	334	37,897
	10 20 30 40 50 60 MKNRVISLLM ASLLLVLSVI VAPFYKAEAA TVVNTPFVAV FSNFDSSQWE KADWANGSVF 70 80 90 100 110 120 NCVWKPSQVT FSNGKMILTL DREYGGSYPY KSGEYRTKSF FGYGYYEVRM KAAKNVGIVS 130 140 150 160 170 180 SFFTYTGPSD NNPWDEIDIE FLGKDTTKVQ FNWYKNGVGG NEYLHNLGFD ASQDFHTYGF 190 200 210 220 230 240 EWRPDYIDFY VDGKKVYRGT RNIPVTPGKI MMNLWPGIGV DEWLGRYDGR TPLQAEYEYV 250 260 270 280 290 300 KYYPNGVPQD NPTPTPTIAP STPTNPNLPL KGDVNGDGHV NSSDYSLFKR YLLRVIDRFP 310 320 330 VGDQSVADVN RDGRIDSTDL TMLKRYLIRA IPSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the Clostridium thermocellum gene licB and the encoded beta-1,3-1,4-glucanase. A catalytic region homologous to Bacillus lichenases joined to the reiterated domain of clostridial cellulases." Schimming S., Schwarz W.H., Staudenbauer W.L. Eur. J. Biochem. 204:13-19(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete sequence of Clostridium thermocellum ATCC 27405." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., Newcomb M., Richardson P. Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27405 / DSM 1237.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X63355 Genomic DNA. Translation: CAA44959.1. CP000568 Genomic DNA. Translation: ABN51452.1.
PIR	S23498.
RefSeq	YP_001036645.1. NC_009012.1.
3D structure databases
ProteinModelPortal	A3DBX3.
SMR	A3DBX3. Positions 41-245.
ModBase	Search...
Protein-protein interaction databases
STRING	203119.Cthe_0211.
Protein family/group databases
CAZy	GH16. Glycoside Hydrolase Family 16.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABN51452; ABN51452; Cthe_0211.
GeneID	4808629.
KEGG	cth:Cthe_0211.
PATRIC	19514051. VBICloThe47081_0224.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2273.
HOGENOM	HOG000250723.
OMA	NSAFFTY.
Enzyme and pathway databases
BioCyc	CTHE203119:GIW8-216-MONOMER. MetaCyc:MONOMER-16465.
Family and domain databases
Gene3D	1.10.1330.10. 1 hit. 2.60.120.200. 1 hit.
InterPro	IPR008264. Beta_glucanase. IPR016134. Cellulos_enz_dockerin_1. IPR002105. Cellulos_enz_dockerin_1_Ca-bd. IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. IPR018242. Dockerin_1. IPR018247. EF_Hand_1_Ca_BS. IPR000757. Glyco_hydro_16. IPR008263. Glycoside_hydrolase_16_AS. [Graphical view]
Pfam	PF00404. Dockerin_1. 2 hits. PF00722. Glyco_hydro_16. 1 hit. [Graphical view]
PRINTS	PR00737. GLHYDRLASE16.
SUPFAM	SSF63446. Cellulos_enz_dockerin_1. 1 hit. SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS00448. CLOS_CELLULOSOME_RPT. 2 hits. PS00018. EF_HAND_1. 2 hits. Uncertain. PS01034. GLYCOSYL_HYDROL_F16. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUB_CLOTH

Accession

Primary (citable) accession number: A3DBX3
Secondary accession number(s): P29716, P37074

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 17, 2007
Last sequence update:	March 20, 2007
Last modified:	May 1, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program