P13860 (GUX1_PHACH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Exoglucanase 1
EC=3.2.1.91

Alternative name(s):
1,4-beta-cellobiohydrolase
Exocellobiohydrolase I
Exoglucanase I

Gene names

Name:

CBH1

Organism

Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)

Taxonomic identifier

5306 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Agaricomycetes › Agaricomycetes incertae sedis › Corticiales › Corticiaceae › Phanerochaete

Protein attributes

Sequence length	516 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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	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
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 – 18	18	Potential
	Chain	19 – 516	498	Exoglucanase 1		PRO_0000007924
Regions
	Domain	480 – 516	37	CBM1
	Region	? – 449		Catalytic
	Region	450 – 480	31	Linker
Sites
	Active site	225	1	Nucleophile By similarity
	Active site	230	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	208	1	N-linked (GlcNAc...) Potential
	Glycosylation	326	1	N-linked (GlcNAc...) Potential
	Glycosylation	442	1	N-linked (GlcNAc...) Potential
	Disulfide bond	488 ↔ 505		By similarity
	Disulfide bond	499 ↔ 515		By similarity
Experimental info
	Sequence conflict	27 – 28	2	RS → EN Ref.1
	Sequence conflict	30 – 31	2	PA → RT Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P13860 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 1C7C3D338ECE1B72	FASTA	516	54,858
	10 20 30 40 50 60 MFRTATLLAF TMAAMVFGQQ VGTNTARSHP ALTSQKCTKS GGCSNLNTKI VLDANWRWLH 70 80 90 100 110 120 STSGYTNCYT GNQWDATLCP DGKTCAANCA LDGADYTGTY GITASGSSLK LQFVTGSNVG 130 140 150 160 170 180 SRVYLMADDT HYQMFQLLNQ EFTFDVDMSN LPCGLNGALY LSAMDADGGM AKYPTNKAGA 190 200 210 220 230 240 KYGTGYCDSQ CPRDIKFING EANVEGWNAT SANAGTGNYG TCCTEMDIWE ANNDAAAYTP 250 260 270 280 290 300 HPCTTNAQTR CSGSDCTRDT GLCDADGCDF NSFRMGDQTF LGKGLTVDTS KPFTVVTQFI 310 320 330 340 350 360 TNDGTSAGTL TEIRRLYVQN GKVIQNSSVK IPGIDPVNSI TDNFCSQQKT AFGDTNYFAQ 370 380 390 400 410 420 HGGLKQVGEA LRTGMVLALS IWDDYAANML WLDSNYPTNK DPSTPGVARG TCATTSGVPA 430 440 450 460 470 480 QIEAQSPNAY VVFSNIKFGD LNTTYTGTVS SSSVSSSHSS TSTSSSHSSS STPPTQPTGV 490 500 510 TVPQWGQCGG IGYTGSTTCA SPYTCHVLNP YYSQCY

References

[1]	"The identification, molecular cloning and characterisation of a gene from Phanerochaete chrysosporium that shows strong homology to the exo-cellobiohydrolase I gene from Trichoderma reesei." Sims P.F.G., James C., Broda P. Gene 74:411-422(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 34541 / NBRC 31249 / ME-446 / PRL 2750.
[2]	"Differential expression of multiple exo-cellobiohydrolase I-like genes in the lignin-degrading fungus Phanerochaete chrysosporium." Sims P.F.G., Soares-Felipe M.S., Wang Q., Gent M.E., Tempelaars C., Broda P. Mol. Microbiol. 12:209-216(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ATCC 34541 / NBRC 31249 / ME-446 / PRL 2750.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M22220 Genomic DNA. Translation: AAB46373.1. Z22528 mRNA. Translation: CAA80253.1.
PIR	JS0083. S33164.
3D structure databases
ProteinModelPortal	P13860.
SMR	P13860. Positions 19-448.
ModBase	Search...
Protein family/group databases
CAZy	CBM1. Carbohydrate-Binding Module Family 1. GH7. Glycoside Hydrolase Family 7.
mycoCLAP	CBH7A_PHACH.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	NOG85664.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-17639.
Family and domain databases
Gene3D	2.70.100.10. 1 hit.
InterPro	IPR000254. Cellulose-bd_dom_fun. IPR008985. ConA-like_lec_gl_sf. IPR001722. Glyco_hydro_7. [Graphical view]
Pfam	PF00734. CBM_1. 1 hit. PF00840. Glyco_hydro_7. 1 hit. [Graphical view]
PRINTS	PR00734. GLHYDRLASE7.
ProDom	PD001821. CBD_fun. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00236. fCBD. 1 hit. [Graphical view]
SUPFAM	SSF57180. CBD_fun. 1 hit. SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS00562. CBM1_1. 1 hit. PS51164. CBM1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUX1_PHACH

Accession

Primary (citable) accession number: P13860

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	April 3, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program