Reviewed, UniProtKB/Swiss-Prot P62695 (GUX1_TRIKO)

Names and origin

Protein names

Recommended name:
    Exoglucanase 1
    EC=3.2.1.91
Alternative name(s):
    Exoglucanase I
    Exocellobiohydrolase I
      Short name=CBHI
    1,4-beta-cellobiohydrolase

Gene names

Name:

cbh1

Organism

Trichoderma koningii (Hypocrea koningii)

Taxonomic identifier

97093 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Hypocreaceae › Hypocrea

Protein attributes

Sequence length	513 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	Hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.
Subcellular location	Secreted.
Sequence similarities	Belongs to the glycosyl hydrolase 7 (cellulase C) family. Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.

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	cellulose 1,4-beta-cellobiosidase 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 – 17	17	By similarity
	Chain	18 – 513	496	Exoglucanase 1		PRO_0000007926
Regions
	Domain	477 – 513	37	CBM1
	Region	18 – 453	436	Catalytic
	Region	454 – 477	24	Linker
Sites
	Active site	143	1	By similarity
	Active site	229	1	Nucleophile By similarity
	Active site	234	1	Proton donor By similarity
Amino acid modifications
	Modified residue	18	1	Pyrrolidone carboxylic acid By similarity
	Glycosylation	62	1	N-linked (GlcNAc...) Potential
	Glycosylation	81	1	N-linked (GlcNAc...) Potential
	Glycosylation	287	1	N-linked (GlcNAc...) Potential
	Glycosylation	401	1	N-linked (GlcNAc...) Potential
	Disulfide bond	21 ↔ 89		By similarity
	Disulfide bond	36 ↔ 42		By similarity
	Disulfide bond	67 ↔ 88		By similarity
	Disulfide bond	78 ↔ 84		By similarity
	Disulfide bond	155 ↔ 414		By similarity
	Disulfide bond	189 ↔ 227		By similarity
	Disulfide bond	193 ↔ 226		By similarity
	Disulfide bond	247 ↔ 273		By similarity
	Disulfide bond	255 ↔ 260		By similarity
	Disulfide bond	278 ↔ 348		By similarity
	Disulfide bond	485 ↔ 502		By similarity
	Disulfide bond	496 ↔ 512		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P62695-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 9F5C0A8A854F2C12	FASTA	513	54,073
	10 20 30 40 50 60 MYRKLAVISA FLATARAQSA CTLQSETHPP LTWQKCSSGG TCTQQTGSVV IDANWRWTHA 70 80 90 100 110 120 TNSSTNCYDG NTWSSTLCPD NETCAKNCCL DGAAYASTYG VTTSGNSLSI GFVTQSAQKN 130 140 150 160 170 180 VGARLYLMAS DTTYQEFTLL GNEFSFDVDV SQLPCGLNGA LYFVSMDADG GVSKYPTNTA 190 200 210 220 230 240 GAKYGTGYCD SQCPRDLKFI NGQANVEGWE PSSNNANTGI GGHGSCCSEM DIWEANSISE 250 260 270 280 290 300 ALTPHPCTTV GQEICEGDGC GGTYSDNRYG GTCDPDGCDW NPYRLGNTSF YGPGSSFTLD 310 320 330 340 350 360 TTKKLTVVTQ FETSGAINRY YVQNGVTFQQ PNAELGSYSG NELNDDYCTA EEAEFGGSSF 370 380 390 400 410 420 SDKGGLTQFK KATSGGMVLV MSLWDDYYAN MLWLDSTYPT NETSSTPGAV RGSCSTSSGV 430 440 450 460 470 480 PAQVESQSPN AKVTFSNIKF GPIGSTGNPS GGNPPGGNRG TTTTRRPATT TGSSPGPTQS 490 500 510 HYGQCGGIGY SGPTVCASGT TCQVLNPYYS QCL

References

[1]	"Molecular cloning and sequence analysis of the cellobiohydrolase I gene from Trichoderma koningii G-39." Wey T.T., Hseu T.H., Huang L. Curr. Microbiol. 28:31-39(1994) [PubMed: 7764306] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: G-39.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X69976 Genomic DNA. Translation: CAA49596.1.
3D structure databases
SMR	P62695. Positions 18-451.
ModBase	Search...
Protein family/group databases
CAZy	CBM1. Carbohydrate-Binding Module Family 1. GH7. Glycoside Hydrolase Family 7.
Enzyme and pathway databases
BRENDA	3.2.1.91. 97070.
Family and domain databases
InterPro	IPR000254. CBD_fun. IPR001722. Glyco_hydro_7. [Graphical view]
Gene3D	G3DSA:2.70.100.10. Glyco_hydro_7. 1 hit.
Pfam	PF00734. CBM_1. 1 hit. PF00840. Glyco_hydro_7. 1 hit. [Graphical view]
PRINTS	PR00734. GLHYDRLASE7.
ProDom	PD001821. CBD_fungal. 1 hit. PD186135. Glyco_hydro_7. 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. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUX1_TRIKO

Accession

Primary (citable) accession number: P62695
Secondary accession number(s): P00725

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)