Reviewed, UniProtKB/Swiss-Prot P15885 (BGLS_RUMAL)

Names and origin

Protein names	Recommended name:     Beta-glucosidase     EC=3.2.1.21 Alternative name(s):     Gentiobiase     Cellobiase     Beta-D-glucoside glucohydrolase
Organism	Ruminococcus albus
Taxonomic identifier	1264 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Clostridia › Clostridiales › Ruminococcaceae › Ruminococcus

Protein attributes

Sequence length	947 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Pathway	Glycan metabolism; cellulose degradation.
Sequence similarities	Belongs to the glycosyl hydrolase 3 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 947	947	Beta-glucosidase		PRO_0000210779
Sites
	Active site	696	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P15885-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: C43B8CDD9D60A115	FASTA	947	104,278
	10 20 30 40 50 60 MIKLDWNEYL EKAAEVNAEG AVLLVNNGVL PLDKNAVTQV FGRIQLDYYK SGTGSGGMVN 70 80 90 100 110 120 VAKVTGITDG LIEAGAKLNE DVLKAYKDYV AEHPYDYGEG WGGEPWCQEE MPLDDSLVKR 130 140 150 160 170 180 AAESSDTAIC IIGRTAGEEQ DNSCKAGSYL LTDGEKAILR KVRDNFSKMV ILLNVGNIID 190 200 210 220 230 240 MGFIDEFSPD AVMYVWQGGM TGGTGTARVL LGEVSPCGKL PDTIAYDITD YPSDKNFHNR 250 260 270 280 290 300 DVDIYAEDIF VGYRYFDTFA KDRVRFPFGY GLSYTQFEIS AEGRKTDDGV VITAKVKNIG 310 320 330 340 350 360 SAAGKEVVQV YLEAPNCKLG KAARVLCGFE KTKVLAPNEE QTLTIEVTER DIASYDDSGI 370 380 390 400 410 420 TGNAFAWVEE AGEYTFYAGS DVRSAKECFA FTLDSTKVIE QLEQALAPVT PFKRMVRTAE 430 440 450 460 470 480 GLSYEDTPLS KVDEAARRLG YLPAETAYTG DKGIALSDVA HGKNTLDEFI AQLDDNDLNC 490 500 510 520 530 540 LVRGEGMCSP KVTPGTAAAF GGVAKHLEEL GIPAGCCSDG PSGMRLDVGT KAFSLPNGTL 550 560 570 580 590 600 IAATFNKSLI TELFTYLGLE MRANKVDCLL GPGMNIHRHP LNGRNFEYFS EDPFLTGTMA 610 620 630 640 650 660 AAELEGLHSV GVEGTIKHFC ANNQETNRHF IDSVASERAL REIYLKGFEI AVRKSKARSV 670 680 690 700 710 720 MTTYGKVNGL WTAGSFDLNT MILRKQWGFD GFTMTDWWAN INDRGCAPDK NNFAAMVRAQ 730 740 750 760 770 780 NDVYMVCADG ESGSDNVIAA LADGRLTRAE LQRSARNILS FMMSTHAMAR KLGEDEAVEV 790 800 810 820 830 840 INKPAETVDD GEGDRVFLLD GDLTIDMSGV KTERNLDYSF TVDVAQFGQY RMEMTASSTQ 850 860 870 880 890 900 SELAQMPVTV FSMGTAWGTF TWNGTGGKPV TFAVEEMPMF SRYTIFRLHF GLGGLDMDKI 910 920 930 940 VFKKIRPAEA QVCRLRISER WLQTQTYFWL KANFQSKKLL RGRRAYR

References

[1]	"DNA sequence of a beta-glucosidase from Ruminococcus albus." Ohmiya K., Takano M., Shimizu S. Nucleic Acids Res. 18:671-671(1990) [PubMed: 2106673] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: F-40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X15415 Genomic DNA. Translation: CAA33461.1.
PIR	S08243.
3D structure databases
SMR	P15885. Positions 509-765.
ModBase	Search...
Protein family/group databases
CAZy	GH3. Glycoside Hydrolase Family 3.
Enzyme and pathway databases
BRENDA	3.2.1.21. 1267.
Family and domain databases
InterPro	IPR019800. Glyco_hydro_3_AS. IPR002772. Glyco_hydro_3_C. IPR001764. Glyco_hydro_3_N. IPR017853. Glyco_hydro_catalytic_core. [Graphical view]
Gene3D	G3DSA:3.20.20.300. Glyco_hydro_3_N. 1 hit.
Pfam	PF00933. Glyco_hydro_3. 1 hit. PF01915. Glyco_hydro_3_C. 1 hit. [Graphical view]
PRINTS	PR00133. GLHYDRLASE3.
PROSITE	PS00775. GLYCOSYL_HYDROL_F3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BGLS_RUMAL

Accession

Primary (citable) accession number: P15885

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	January 19, 2010
This is version 53 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)