Reviewed, UniProtKB/Swiss-Prot P07984 (GUNA_CELFI)

Names and origin

Protein names

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

Gene names

Name:

cenA

Organism

Cellulomonas fimi

Taxonomic identifier

1708 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Cellulomonadaceae › Cellulomonas

Protein attributes

Sequence length	449 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)

Function	The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Post-translational modification	The linker region (also termed "hinge") may be a potential site for proteolysis. Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
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 – 31	31	Tat-type signal Potential
	Chain	32 – 449	418	Endoglucanase A		PRO_0000007903
Regions
	Domain	32 – 137	106	CBM2
	Region	139 – 168	30	Linker ("hinge") (Pro-Thr box)
	Region	438 – 449	12	Catalytic
Sites
	Active site	247	1	By similarity
	Active site	283	1	Proton donor By similarity
	Active site	423	1	Nucleophile By similarity
Amino acid modifications
	Disulfide bond	35 ↔ 134		Ref.3
	Disulfide bond	248 ↔ 291		Ref.3
	Disulfide bond	390 ↔ 426		Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P07984-1 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 67FF887814B3348D	FASTA	449	46,731
	10 20 30 40 50 60 MSTRRTAAAL LAAAAVAVGG LTALTTTAAQ AAPGCRVDYA VTNQWPGGFG ANVTITNLGD 70 80 90 100 110 120 PVSSWKLDWT YTAGQRIQQL WNGTASTNGG QVSVTSLPWN GSIPTGGTAS FGFNGSWAGS 130 140 150 160 170 180 NPTPASFSLN GTTCTGTVPT TSPTPTPTPT TPTPTPTPTP TPTPTVTPQP TSGFYVDPTT 190 200 210 220 230 240 QGYRAWQAAS GTDKALLEKI ALTPQAYWVG NWADASHAQA EVADYTGRAV AAGKTPMLVV 250 260 270 280 290 300 YAIPGRDCGS HSGGGVSESE YARWVDTVAQ GIKGNPIVIL EPDALAQLGD CSGQGDRVGF 310 320 330 340 350 360 LKYAAKSLTL KGARVYIDAG HAKWLSVDTP VNRLNQVGFE YAVGFALNTS NYQTTADSKA 370 380 390 400 410 420 YGQQISQRLG GKKFVIDTSR NGNGSNGEWC NPRGRALGER PVAVNDGSGL DALLWVKLPG 430 440 ESDGACNGGP AAGQWWQEIA LEMARNARW

References

[1]	"Characterization and structure of an endoglucanase gene cenA of Cellulomonas fimi." Wong W.K.R., Gerhard B., Guo Z.M., Kilburn D.G., Warren R.A.J., Miller R.C. Jr. Gene 44:315-324(1986) [PubMed: 3023193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Structural and functional analysis of a bacterial cellulase by proteolysis." Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J. J. Biol. Chem. 264:17802-17808(1989) [PubMed: 2681184] [Abstract] Cited for: DOMAINS.
[3]	"Structural and functional relationships in two families of beta-1,4-glycanases." Gilkes N.R., Claeyssens M., Aebersold R., Henrissat B., Meinke A., Morrison H.D., Kilburn D.G., Warren R.A.J., Miller R.C. Jr. Eur. J. Biochem. 202:367-377(1991) [PubMed: 1761039] [Abstract] Cited for: DISULFIDE BONDS.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M15823 Genomic DNA. Translation: AAA23084.1.
PIR	A24993.
3D structure databases
HSSP	HSSP built from PDB template 1EXG based on UniProtKB P07986.
ModBase	Search...
Protein family/group databases
CAZy	CBM2. Carbohydrate-Binding Module Family 2. GH6. Glycoside Hydrolase Family 6.
Enzyme and pathway databases
BRENDA	3.2.1.4. 97800.
Family and domain databases
InterPro	IPR016288. Beta_cellobiohydrolase. IPR001919. CBD_bac. IPR012291. CBD_carb_bd. IPR018366. CBM2_CS. IPR001524. Glyco_hydro_6_CS. IPR017909. Twin_arg_translocation_Tat. [Graphical view]
Gene3D	G3DSA:2.60.40.290. CBD_carb_bd. 1 hit. G3DSA:3.20.20.40. Glyco_hydro_6. 1 hit.
Pfam	PF00553. CBM_2. 1 hit. PF01341. Glyco_hydro_6. 1 hit. [Graphical view]
PIRSF	PIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTS	PR00733. GLHYDRLASE6.
ProDom	PD003733. Glyco_hydro_6. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00637. CBD_II. 1 hit. [Graphical view]
PROSITE	PS51173. CBM2. 1 hit. PS00561. CBM2_A. 1 hit. PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit. PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit. PS51318. TAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUNA_CELFI

Accession

Primary (citable) accession number: P07984

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	June 16, 2009
This is version 78 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)