Reviewed, UniProtKB/Swiss-Prot P50900 (GUX2_CLOSR)

Names and origin

Protein names

Recommended name:
    Exoglucanase-2
    EC=3.2.1.91
Alternative name(s):
    Exoglucanase II
    Exocellobiohydrolase II
    1,4-beta-cellobiohydrolase II
    Avicelase II

Gene names

Name:

celY

Organism

Clostridium stercorarium

Taxonomic identifier

1510 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	914 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.
Sequence similarities	Belongs to the glycosyl hydrolase 48 (cellulase L) family. Contains 1 CBM3 (carbohydrate binding type-3) domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro cellulose 1,4-beta-cellobiosidase 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 – 33	33	Potential
	Chain	34 – 914	881	Exoglucanase-2		PRO_0000008030
Regions
	Domain	763 – 914	152	CBM3

Sequences

	Sequence		Length	Mass (Da)
	P50900-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: D0DB6017D6DFF82C	FASTA	914	103,021
	10 20 30 40 50 60 MKRRLMKGIS LLTLVFLIGI MLQLSLKSEL TAYASSDDPY KQRFLELWEE LHDPSNGYFS 70 80 90 100 110 120 SHGIPYHAVE TLIVEAPDYG HLTTSEAMSY YLWLEALYGK FTGDFSYFMK AWETIEKYMI 130 140 150 160 170 180 PTEQDQPNRS MAGYNPAKPA TYAPEWEEPS MYPSQLDFSA PVGIDPIYNE LVSTYGTNTI 190 200 210 220 230 240 YGMHWLLDVD NWYGFGRRAD RISSPAYINT FQRGSQESVW ETIPQPCWDD LTIGGRNGFL 250 260 270 280 290 300 DLFVGDSQYS AQFKYTNAPD ADARAIQATY WANQWAKEHG VNLSQYVKKA SRMGDYLRYA 310 320 330 340 350 360 MFDKYFRKIG DSKQAGTGYD AAHYLLSWYY AWGGGITADW AWIIGCSHVH AGYQNPMTAW 370 380 390 400 410 420 ILANDPEFKP ESPNGANDWA KSLERQLEFY QWLQSAEGAI AGGATNSYKG RYETLPAGIS 430 440 450 460 470 480 TFYGMAYEEH PVYLDPGSNT WFGFQAWTMQ RVAEYYYLTG DTRAEQLLDK WVDWIKSVVR 490 500 510 520 530 540 LNSDGTFEIP GNLEWSGQPD TWTGTYTGNP NLHVSVVSYR TDLGAAGSLA NALLYYAKTS 550 560 570 580 590 600 GDDEARNLAK ELLDRMWNLY RDDKGLSAPE TREDYVRFFE QEVYVPQGWS GTMPNGDRIE 610 620 630 640 650 660 PGVTFLDIRS KYLNDPDYPK LQQAYNEGKA PVFNYHRFWA QCDIAIANGL YSILFGSEQA 670 680 690 700 710 720 NDSFITPTSA TFDKNNQEDI SVTVTYNGNT LLGIKSGSSY LIEGVDYIVN GDVIIIKKEF 730 740 750 760 770 780 LAGQATGSIS LLFDFSAGLD RTLTIDIIDT GGGEEPVEPV EPVEGVLIIQ SFNANTQEIS 790 800 810 820 830 840 NSIMPRFRIY NSGNTSIPLS EVKLRYYYTV DGDKPQNFWC DWASIGSSNV TGTFVKMDGA 850 860 870 880 890 900 TTGADYYLEI GFTPQAGTLE PGASIEVQGR FSKIDWTDYT QTNDYSFNPT ASSYVDFNKI 910 TAYISGNLVY GIEP

References

[1]	Bronnenmeier K., Kundt K., Riedel K., Schwarz W.H., Staudenbauer W.L. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NCIB 11754.
[2]	"Purification and properties of a novel type of exo-1,4-beta-glucanase (avicelase II) from the cellulolytic thermophile Clostridium stercorarium." Bronnenmeier K., Ruecknagel K.P., Staudenbauer W.L. Eur. J. Biochem. 200:379-385(1991) [PubMed: 1909625] [Abstract] Cited for: CHARACTERIZATION. Strain: NCIB 11754.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z69359 Genomic DNA. Translation: CAA93280.1.
3D structure databases
HSSP	HSSP built from PDB template 1FAE based on UniProtKB P37698.
ModBase	Search...
Protein family/group databases
CAZy	CBM3. Carbohydrate-Binding Module Family 3. GH48. Glycoside Hydrolase Family 48.
Enzyme and pathway databases
BRENDA	3.2.1.91. 16695.
Family and domain databases
InterPro	IPR012341. 6hp_glycosidase. IPR001956. CBD_3. IPR005102. DUF291. IPR000556. Glyco_hydro_48F. IPR013783. Ig-like_fold. [Graphical view]
Gene3D	G3DSA:2.60.40.710. CBD_3. 1 hit. G3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit. G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
Pfam	PF00942. CBM_3. 1 hit. PF03442. DUF291. 1 hit. PF02011. Glyco_hydro_48. 1 hit. [Graphical view]
PRINTS	PR00844. GLHYDRLASE48.
ProDom	PD001947. CBD_3. 1 hit. PD011903. Glyco_hydro_48. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS51172. CBM3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUX2_CLOSR

Accession

Primary (citable) accession number: P50900

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 5, 2009
This is version 50 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)