Reviewed, UniProtKB/Swiss-Prot P0C946 (BGLA_THENE)

Names and origin

Protein names

Recommended name:
    Beta-glucosidase A
    EC=3.2.1.21
Alternative name(s):
    Gentiobiase
    Cellobiase
    Beta-D-glucoside glucohydrolase

Gene names

Name:	bglA
Synonyms:	gghA

Organism

Thermotoga neapolitana

Taxonomic identifier

2337 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	425 AA.
Sequence status	Fragment.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	This enzyme has broad substrate specificity By similarity.
Catalytic activity	Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Pathway	Glycan metabolism; cellulose degradation.
Subunit structure	Monomer By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 1 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Molecular function	Glycosidase Hydrolase
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	beta-glucosidase activity Inferred from electronic annotation. Source: EC cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 425	425	Beta-glucosidase A		PRO_0000063880
Sites
	Active site	164	1	Proton donor Potential
	Active site	349	1	Nucleophile By similarity
Experimental info
	Non-terminal residue	425	1

Sequences

	Sequence		Length	Mass (Da)
	P0C946-1 [UniParc]. Last modified May 5, 2009. Version 1. Checksum: E66E33B75266187B	FASTA	425	49,366
	10 20 30 40 50 60 MKKFPEGFLW GVATASYQIE GSPLADGAGM SIWHTFSHTP GNVKNGDTGD VACDHYNRWK 70 80 90 100 110 120 EDIEIIEKIG AKAYRFSISW PRILPEGTGK VNQKGLDFYN RIIDTLLEKN ITPFITIYHW 130 140 150 160 170 180 DLPFSLQLKG GWANRDIADW FAEYSRVLFE NFGDRVKHWI TLNEPWVVAI VGHLYGVHAP 190 200 210 220 230 240 GMKDIYVAFH TVHNLLRAHA KSVKVFRETV KDGKIGIVFN NGYFEPASER EEDIRAARFM 250 260 270 280 290 300 HQFNNYPLFL NPIYRGEYPD LVLEFAREYL PRNYEDDMEE IKQEIDFVGL NYYSGHMVKY 310 320 330 340 350 360 DPNSPARVSF VERNLPKTAM GWEIVPEGIY WILKGVKEEY NPQEVYITEN GAAFDDVVSE 370 380 390 400 410 420 GGKVHDQNRI DYLRAHIEQV WRAIQDGVPL KGYFVWSLLD NFEWAEGYSK RFGIVYVDYN TQKRI

References

[1]	Zverlov V. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Z2706-MC24.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z97212 Genomic DNA. Translation: CAB10165.1.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GH1. Glycoside Hydrolase Family 1.
Enzyme and pathway databases
BRENDA	3.2.1.21. 1590.
Family and domain databases
InterPro	IPR001360. Glyco_hydro_1. IPR018120. Glyco_hydro_1_AS. IPR017736. Glyco_hydro_1_beta-glucosidase. IPR017853. Glyco_hydro_catalytic_core. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHER	PTHR10353. Glyco_hydro_1. 1 hit.
Pfam	PF00232. Glyco_hydro_1. 1 hit. [Graphical view]
PRINTS	PR00131. GLHYDRLASE1.
TIGRFAMs	TIGR03356. BGL. 1 hit.
PROSITE	PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit. PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BGLA_THENE

Accession

Primary (citable) accession number: P0C946
Secondary accession number(s): O33843, O52505

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	May 5, 2009
Last modified:	February 9, 2010
This is version 6 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)