Reviewed, UniProtKB/Swiss-Prot P18336 (GUN_CELUD)

Names and origin

Protein names	Recommended name:     Endoglucanase     EC=3.2.1.4 Alternative name(s):     Endo-1,4-beta-glucanase     Cellulase
Organism	Cellulomonas uda
Taxonomic identifier	1714 [NCBI]
Taxonomic lineage	Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Cellulomonadaceae › Cellulomonas

Protein attributes

Sequence length	359 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.
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
Technical term	Direct protein sequencing
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 – 23	23	Ref.1
	Chain	24 – 359	336	Endoglucanase		PRO_0000007933
Sites
	Active site	53	1	Proton donor By similarity
	Active site	110	1	Nucleophile Potential

Sequences

	Sequence		Length	Mass (Da)
	P18336-1 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: 0445D7571B683148	FASTA	359	40,690
	10 20 30 40 50 60 MPLRALVAVI VTTAVMLVPR AWAQTAWERY KARFMMPDAR IIDTANGNVS HTEGQGFAML 70 80 90 100 110 120 LAVANNDRPA FDKLWQWTDS TLRDKSNGLF YWRYNPVAPD PIADKNNATD GDTLIAWALL 130 140 150 160 170 180 RAQKQWQDKR YATASDAITA SLLKYTVVTF AGRQVMLPGV KGFNRNDHLN LNPSYFIFPA 190 200 210 220 230 240 WRAFAERTHL TAWRTLQSDG QALLGQMGWG KSHLPSDWVA LRADGKMLPA KEWPPRMSFD 250 260 270 280 290 300 AIRIPLYISW VDPHSALLAP WKAWMQSYPR LQTPAWINVS TNEVAPWNMA GGLLAVRDLT 310 320 330 340 350 LGEPLERRRL TTRMIITPPA SSCWSGWRNR ISASAVMALQ VSQPVCLRAE RKEQERLTM

References

[1]	"Sequence of a cellulase gene of Cellulomonas uda CB4." Nakamura K., Misawa N., Kitamura K. J. Biotechnol. 4:247-254(1986) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-37. Strain: CB4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M36503 Genomic DNA. Translation: AAA23090.1.
PIR	I40696.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GH8. Glycoside Hydrolase Family 8.
Enzyme and pathway databases
BRENDA	3.2.1.4. 97424.
Family and domain databases
InterPro	IPR012341. 6hp_glycosidase. IPR002037. Glyco_hydro_8. IPR019834. Glyco_hydro_8_CS. [Graphical view]
Gene3D	G3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit.
Pfam	PF01270. Glyco_hydro_8. 1 hit. [Graphical view]
PRINTS	PR00735. GLHYDRLASE8.
PROSITE	PS00812. GLYCOSYL_HYDROL_F8. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUN_CELUD

Accession

Primary (citable) accession number: P18336

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	June 16, 2009
This is version 55 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)