Reviewed, UniProtKB/Swiss-Prot P37701 (GUN2_CLOJO)

Names and origin

Protein names

Recommended name:
    Endoglucanase 2
    EC=3.2.1.4
Alternative name(s):
    Endo-1,4-beta-glucanase 2
    Cellulase 2

Gene names

Name:

celB

Organism

Clostridium josui

Taxonomic identifier

1499 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	460 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	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence similarities	Belongs to the glycosyl hydrolase 8 (cellulase D) family.

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	cellulase 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 – 32	32	Potential
	Chain	33 – 460	428	Endoglucanase 2		PRO_0000007934
Sites
	Active site	99	1	Proton donor By similarity
	Active site	155	1	Nucleophile Potential

Sequences

	Sequence		Length	Mass (Da)
	P37701-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 65EEAABCD82B7BD4	FASTA	460	50,599
	10 20 30 40 50 60 MIKGSSLKRI KSLVMMAIFS VSIITTAIVS SAADQIPFPY NATYPYGAYS CLADSQSSAN 70 80 90 100 110 120 NLLKSEWEQW KSAHITSNGA RGYKRVQRDA STNYDTVSEG LGYGMLLAVY FGEQQLFDDL 130 140 150 160 170 180 YRYVKVFLNS NGLMSWRIDA NGNIMGQNAI GAATDADEDI AVSLVFAHKK WGTSGGFNYQ 190 200 210 220 230 240 TEAKNYINNI YNKMVEPGTY VLKPGDMWGG SDVTNPSYFA PAWYRIFADF TGNSGWINVA 250 260 270 280 290 300 NKCYEIADKA RNSNTGLVPD WCTANGTPAS GQGYDFYYDA IRYQWRTAID YSWYGTAKAK 310 320 330 340 350 360 THCDAISNFF KNIGYPNIKD GYTLSGSQIS ANHTATFVSC AAAAAMTGTD ATYAKNIYNE 370 380 390 400 410 420 CVKVKDTGNY TYFGNTLRMM ILLYTTGNFP NLYSYSSQPQ QGLKGDVNND GAIDALDIAA 430 440 450 460 LKKAILTQST SNINLTNADM NNDGNIDAID FAQLKVKLLN

References

[1]	Fujino T., Karita S., Ohmiya K. Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	D16670 Genomic DNA. Translation: BAA04078.1.
PIR	I40799.
3D structure databases
HSSP	HSSP built from PDB template 1IS9 based on UniProtKB P04955.
ModBase	Search...
Protein family/group databases
CAZy	GH8. Glycoside Hydrolase Family 8.
Enzyme and pathway databases
BRENDA	3.2.1.4. 257917.
Family and domain databases
InterPro	IPR012341. 6hp_glycosidase. IPR016134. Cellulos_enz_dockerin_1. IPR002105. Cellulos_enz_dockerin_1_Ca-bd. IPR018242. Dockerin_1. IPR018247. EF_HAND_1. IPR002037. Glyco_hydro_8. IPR019834. Glyco_hydro_8_CS. [Graphical view]
Gene3D	G3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit. G3DSA:1.10.1330.10. Cellulos_enz_dockerin_1. 1 hit.
Pfam	PF00404. Dockerin_1. 2 hits. PF01270. Glyco_hydro_8. 1 hit. [Graphical view]
PRINTS	PR00735. GLHYDRLASE8.
PROSITE	PS00448. CLOS_CELLULOSOME_RPT. 1 hit. PS00018. EF_HAND_1. 2 hits. Uncertain. PS00812. GLYCOSYL_HYDROL_F8. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUN2_CLOJO

Accession

Primary (citable) accession number: P37701

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	June 16, 2009
This is version 57 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)