P26414 (GUNA_THEBI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoglucanase A
EC=3.2.1.4

Alternative name(s):
Cellulase A
Endo-1,4-beta-glucanase A

Gene names

Name:

celA

Organism

Thermobispora bispora (Microbispora bispora)

Taxonomic identifier

2006 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Thermobispora

Protein attributes

Sequence length	456 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 6 (cellulase B) family. Contains 1 CBM2 (carbohydrate binding type-2) domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
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 polysaccharide 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
	Signal peptide	1 – 30	30	Potential
	Chain	31 – 456	426	Endoglucanase A		PRO_0000007905
Regions
	Domain	353 – 456	104	CBM2
	Region	31 – 322	292	Catalytic
	Region	323 – 355	33	Linker ("hinge") (Pro-Ser box)
Sites
	Active site	113	1	By similarity
	Active site	151	1	Proton donor By similarity
	Active site	300	1	Nucleophile By similarity
Amino acid modifications
	Disulfide bond	114 ↔ 159		By similarity
	Disulfide bond	267 ↔ 302		By similarity
	Disulfide bond	360 ↔ 453		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P26414 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: B06D8595E322848F	FASTA	456	47,011
	10 20 30 40 50 60 MSRIRRFLAT ALAAATAGVG AIVTAIASAG PAHAYDSPFY VDPQSNAAKW VAANPNDPRT 70 80 90 100 110 120 PVIRDRIAAV PTGRWFANYN PSTVRAEVDA YVGAAAAAGK IPIMVVYAMP NRDCGGPSAG 130 140 150 160 170 180 GAPNHTAYRA WIDEIAAGLR NRPAVIILEP DALPIMTNCM SPSEQAEVQA SAVGAGKKFK 190 200 210 220 230 240 AASSQAKVYF DAGHDAWVPA DEMASRLRGA DIANSADGIA LNVSNYRYTS GLISYAKSVL 250 260 270 280 290 300 SAIGASHLRA VIDTSRNGNG PLGSEWCDPP GRATGTWSTT DTGDPAIDAF LWIKPPGEAD 310 320 330 340 350 360 GCIATPGVFV PDRAYELAMN AAPPTYSPSP TPSTPSPSPS QSDPGSPSPS PSQPPAGRAC 370 380 390 400 410 420 EATYALVNQW PGGFQAEVTV KNTGSSPING WTVQWTLPSG QSITQLWNGD LSTSGSNVTV 430 440 450 RNVSWNGNVP AGGSTSFGFL GSGTGQLSSS ITCSAS

References

[1]	Yablonsky M.D., Elliston K.O., Eveleigh D.E. (In) Coughlan M.P. (eds.); Production, characterization and application of cellulose, hemicellulose and lignin enzyme degrading systems, pp.77-83, Elsevier, London (1989) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

3D structure databases
ProteinModelPortal	P26414.
SMR	P26414. Positions 36-321, 356-449.
ModBase	Search...
Protein family/group databases
CAZy	CBM2. Carbohydrate-Binding Module Family 2. GH6. Glycoside Hydrolase Family 6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	2.60.40.290. 1 hit. 3.20.20.40. 1 hit.
InterPro	IPR016288. Beta_cellobiohydrolase. IPR008965. Carb-bd_dom. IPR012291. CBD_carb-bd_dom. IPR018366. CBM2_CS. IPR001919. Cellulose-bd_dom_fam2_bac. IPR001524. Glyco_hydro_6_CS. [Graphical view]
Pfam	PF00553. CBM_2. 1 hit. PF01341. Glyco_hydro_6. 1 hit. [Graphical view]
PRINTS	PR00733. GLHYDRLASE6.
SMART	SM00637. CBD_II. 1 hit. [Graphical view]
SUPFAM	SSF49384. Cellul_bind. 1 hit. SSF51989. Glyco_hydro_6. 1 hit.
PROSITE	PS51173. CBM2. 1 hit. PS00561. CBM2_A. 1 hit. PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit. PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUNA_THEBI

Accession

Primary (citable) accession number: P26414

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	March 6, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program