Q12622 (GUN1_HUMGT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoglucanase EG-1
EC=3.2.1.4

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

Gene names

Name:

EG-1

Organism

Humicola grisea var. thermoidea

Taxonomic identifier

5528 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › mitosporic Ascomycota › Humicola › Humicola grisea

Protein attributes

Sequence length	435 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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.
Subcellular location	Secreted.
Sequence similarities	Belongs to the glycosyl hydrolase 7 (cellulase C) family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	By similarity
	Chain	21 – 435	415	Endoglucanase EG-1		PRO_0000007916
Sites
	Active site	217	1	Nucleophile By similarity
	Active site	222	1	Proton donor By similarity
Amino acid modifications
	Modified residue	21	1	Pyrrolidone carboxylic acid By similarity
	Glycosylation	109	1	N-linked (GlcNAc...) By similarity
	Glycosylation	267	1	N-linked (GlcNAc...) By similarity
	Disulfide bond	38 ↔ 44		By similarity
	Disulfide bond	71 ↔ 93		By similarity
	Disulfide bond	83 ↔ 89		By similarity
	Disulfide bond	160 ↔ 385		By similarity
	Disulfide bond	192 ↔ 215		By similarity
	Disulfide bond	196 ↔ 214		By similarity
	Disulfide bond	235 ↔ 254		By similarity
	Disulfide bond	243 ↔ 248		By similarity
	Disulfide bond	259 ↔ 335		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q12622 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 25EB3D62D96B65FA	FASTA	435	47,890
	10 20 30 40 50 60 MARGTALLGL TSLLLGLVNG QKPGETKEVH PQLTTFRCTK KGGCKPATNY IVLDSLSHPI 70 80 90 100 110 120 HRAEGLGWGN CGDWGNPPPK DVCPDVESCA KNCIMEGIPD YSQYGVTTNG TSLRLQHILP 130 140 150 160 170 180 DGRVPSPRVY LLDKTERRYE MLHLTGFEFT FDVDATKLPC GMNSALYLSE MHPTGAKSKH 190 200 210 220 230 240 NPGGAYYGTG YCDAQCFVTP FINGLGNIEG KGSCCNEMDI WEANSRASHV APHVCNKKGL 250 260 270 280 290 300 YLCEGEECAF EGVCDKNGCG WNPYRVNVTD YYGRGEEFKV NTLKPFTVVT QFLANRKGKL 310 320 330 340 350 360 EKIHRFYVQD GKIIESFYTN KEGIPYTNMI EDEFCAATGS RKYMELGATQ GMGEALTRGM 370 380 390 400 410 420 VLAMSIWWDQ GGNMEWLDHG EAGPCAKGEG APSNVVQVEP FPEVTYTNLR WGEIGSTYQE 430 VQKPKPKPGP GPRSD

References

[1]	Takashima S., Nakamura A., Hidaka M., Masaki H., Uozumi T. Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: IFO 9854.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D63516 Genomic DNA. Translation: BAA09786.1.
3D structure databases
ProteinModelPortal	Q12622.
SMR	Q12622. Positions 21-418.
ModBase	Search...
Protein family/group databases
CAZy	GH7. Glycoside Hydrolase Family 7.
mycoCLAP	EGL7A_HUMGT.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	2.70.100.10. 1 hit.
InterPro	IPR008985. ConA-like_lec_gl_sf. IPR001722. Glyco_hydro_7. [Graphical view]
Pfam	PF00840. Glyco_hydro_7. 1 hit. [Graphical view]
PRINTS	PR00734. GLHYDRLASE7.
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GUN1_HUMGT

Accession

Primary (citable) accession number: Q12622

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	March 6, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program