Q59394 (GUNN_ERWCR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoglucanase N
EC=3.2.1.4

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

Gene names

Name:

celN

Organism

Erwinia carotovora subsp. atroseptica (Pectobacterium atrosepticum)

Taxonomic identifier

29471 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium

Protein attributes

Sequence length	444 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.
Subcellular location	Secreted.
Sequence similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) family. Contains 1 CBM3 (carbohydrate binding type-3) domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Gene Ontology (GO)
Biological_process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cellulase activity Inferred from electronic annotation. Source: EC cellulose 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	Potential
	Chain	32 – 444	413	Endoglucanase N		PRO_0000007857
Regions
	Domain	356 – 444	89	CBM3
Sites
	Active site	168	1	Proton donor By similarity
	Active site	256	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q59394 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: FA7E4179004CBB43	FASTA	444	48,301
	10 20 30 40 50 60 MWMRRNQIVR KLTLGVVTTV LGMSLSFSAL SATPVETHGQ LSIENGRLVD EQGKRVQLRG 70 80 90 100 110 120 VSSHGLQWFG DYVNKDSMKW LRDDWGINVF RVAMYTAADG YISNPSLANK VKEAVAAAQS 130 140 150 160 170 180 LGVYIIIDWH ILSDNDPNIY KAQAKTFFAE MAGLYGSSPN VIYEIANEPN GGVTWNGQIR 190 200 210 220 230 240 PYALEVTDTI RSKDPDNLII VGTGTWSQDI HDAADNQLPD PNTLYALHFY AGTHGQFLRD 250 260 270 280 290 300 RIDYAQSRGA AIFVSEWGTS DASGNGGPFL PESQTWIDFL NNRGVSWVNW SLTDKSEASA 310 320 330 340 350 360 ALAPGASKSG GWTEQNLSTS GKFVREQIRA GANLGGGDTP TTPTTPTEPT NPGNGTTGDV 370 380 390 400 410 420 VLQYRNVDNN PSDDAIRMAV NIKNTGSTPI KLSDLQVRYY FHDDGKPGAN LFVDWANVGP 430 440 NNIVTSTGTP AASTDKANRY VLVT

References

[1]

"Transplanting two unique beta-glucanase catalytic activities into one multienzyme, which forms glucose." Olsen O., Thomsen K.K., Weber J., Duus J.O., Svendsen I., Wegener C., von Wettstein D. Biotechnology (N.Y.) 14:71-76(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	L39788 Genomic DNA. Translation: AAC37033.1.
3D structure databases
ProteinModelPortal	Q59394.
SMR	Q59394. Positions 35-332.
ModBase	Search...
Protein family/group databases
CAZy	CBM3. Carbohydrate-Binding Module Family 3. GH5. Glycoside Hydrolase Family 5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG2730.
Family and domain databases
Gene3D	2.60.40.710. 1 hit. 3.20.20.80. 1 hit.
InterPro	IPR008965. Carb-bd_dom. IPR001956. CBD_3. IPR001547. Glyco_hydro_5. IPR018087. Glyco_hydro_5_CS. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF00942. CBM_3. 1 hit. PF00150. Cellulase. 1 hit. [Graphical view]
SMART	SM01067. CBM_3. 1 hit. [Graphical view]
SUPFAM	SSF49384. Cellul_bind. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS51172. CBM3. 1 hit. PS00659. GLYCOSYL_HYDROL_F5. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUNN_ERWCR

Accession

Primary (citable) accession number: Q59394

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program