Reviewed, UniProtKB/Swiss-Prot Q12624 (GUN3_HUMIN)

Names and origin

Protein names

Recommended name:
    Endoglucanase 3
    EC=3.2.1.4
Alternative name(s):
    Endo-1,4-beta-glucanase 3
    Cellulase 3

Gene names

Name:

CMC3

Organism

Humicola insolens

Taxonomic identifier

34413 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › mitosporic Ascomycota › Humicola

Protein attributes

Sequence length	388 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)

Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Biotechnological use	Used as a detergent cellulase. Sold under the name Celluzyme by Novozymes. This special enzyme has three effects: colour brightening, softening and removal of particulate soil. The overall effect is that it helps to preserve the nice appearance of new fabric and restores old fabric so that it looks new again.
Sequence similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) family. Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro 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 – 16	16	Potential
	Chain	17 – 388	372	Endoglucanase 3		PRO_0000007863
Regions
	Domain	17 – 52	36	CBM1
	Region	53 – 91	39	Linker
	Region	92 – 388	297	Catalytic
Sites
	Active site	215	1	Proton donor By similarity
	Active site	322	1	Nucleophile By similarity
Amino acid modifications
	Glycosylation	92	1	N-linked (GlcNAc...) Potential
	Glycosylation	155	1	N-linked (GlcNAc...) Potential
	Glycosylation	259	1	N-linked (GlcNAc...) Potential
	Disulfide bond	24 ↔ 41		By similarity
	Disulfide bond	35 ↔ 51		By similarity
Experimental info
	Sequence conflict	8	1	G → S in BAA12676. Ref.2
	Sequence conflict	340	1	T → N in BAA12676. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q12624-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: C7CF349DACC10690	FASTA	388	42,564
	10 20 30 40 50 60 MKHSVLAGLF ATGALAQGGA WQQCGGVGFS GSTSCVSGYT CVYLNDWYSQ CQPQPTTLRT 70 80 90 100 110 120 TTTPGATSTT RSAPAATSTT PAKGKFKWFG INQSCAEFGK GEYPGLWGKH FTFPSTSSIQ 130 140 150 160 170 180 THINDGFNMF RVAFSMERLA PNQLNAAFDA NYLRNLTETV NFITGKGKYA MLDPHNFGRY 190 200 210 220 230 240 YERIITDKAA FASFFTKLAT HFASNPLVVF DTNNEYHDMD QQLVFDLNQA AIDAIRAAGA 250 260 270 280 290 300 TSQYIMVEGN SWTGAWTWNV TNNNLAALRD PENKLVYQMH QYLDSDGSGT STACVSTQVG 310 320 330 340 350 360 LQRVIGATNW LRQNGKVGLL GEFAGGANSV CQQAIEGMLT HLQENSDVWT GALWWAGGPW 370 380 WGDYIYSFEP PSGIGYTYYN SLLKKYVP

References

[1]	"A novel method for efficient expression cloning of fungal enzyme genes." Dalboege H., Hansen H.P.H. Mol. Gen. Genet. 243:253-260(1994) [PubMed: 8190078] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning, sequencing, and expression of a thermostable cellulase gene of Humicola grisea." Takashima S., Nakamura A., Masaki H., Uozumi T. Biosci. Biotechnol. Biochem. 61:245-250(1997) [PubMed: 9058960] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: IFO 9854.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X76046 Genomic DNA. Translation: CAA53631.1. D84470 Genomic DNA. Translation: BAA12676.1.
PIR	JC5461. S43920.
3D structure databases
HSSP	HSSP built from PDB template 1AZ6 based on UniProtKB P00725.
ModBase	Search...
Protein family/group databases
CAZy	CBM1. Carbohydrate-Binding Module Family 1. GH5. Glycoside Hydrolase Family 5.
Enzyme and pathway databases
BRENDA	3.2.1.4. 1892.
Family and domain databases
InterPro	IPR000254. CBD_fun. IPR001547. Glyco_hydro_5. IPR018087. Glyco_hydro_5_CS. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00734. CBM_1. 1 hit. PF00150. Cellulase. 1 hit. [Graphical view]
ProDom	PD001821. CBD_fungal. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00236. fCBD. 1 hit. [Graphical view]
PROSITE	PS00562. CBM1_1. 1 hit. PS51164. CBM1_2. 1 hit. PS00659. GLYCOSYL_HYDROL_F5. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUN3_HUMIN

Accession

Primary (citable) accession number: Q12624
Secondary accession number(s): Q12620

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 4, 2001
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)