Q9UVS8 (CBHB_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1,4-beta-D-glucan cellobiohydrolase B
EC=3.2.1.91

Alternative name(s):
Beta-glucancellobiohydrolase B
Exocellobiohydrolase B
Exoglucanase B

Gene names

Name:

cbhB

Organism

Aspergillus niger

Taxonomic identifier

5061 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	536 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 By similarity. Ref.2
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 Probable.
Induction	Expression is under the control of the xylanolytic transcriptional activator xlnR. Ref.1 Ref.2
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 – 21	21	Potential
	Chain	22 – 536	515	1,4-beta-D-glucan cellobiohydrolase B		PRO_5000056395
Regions
	Domain	500 – 536	37	CBM1
	Region	22 – 458	437	Catalytic
	Region	459 – 500	42	Ser/Thr-rich linker
Sites
	Active site	233	1	Nucleophile By similarity
	Active site	238	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	351	1	N-linked (GlcNAc...) Potential
	Glycosylation	414	1	N-linked (GlcNAc...) Potential
	Disulfide bond	508 ↔ 525		By similarity
	Disulfide bond	519 ↔ 535		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9UVS8 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: EB904612E2FA3A60	FASTA	536	56,219
	10 20 30 40 50 60 MSSFQIYRAA LLLSILATAN AQQVGTYTTE THPSLTWQTC TSDGSCTTND GEVVIDANWR 70 80 90 100 110 120 WVHSTSSATN CYTGNEWDTS ICTDDVTCAA NCALDGATYE ATYGVTTSGS ELRLNFVTQG 130 140 150 160 170 180 SSKNIGSRLY LMSDDSNYEL FKLLGQEFTF DVDVSNLPCG LNGALYFVAM DADGGTSEYS 190 200 210 220 230 240 GNKAGAKYGT GYCDSQCPRD LKFINGEANC DGWEPSSNNV NTGVGDHGSC CAEMDVWEAN 250 260 270 280 290 300 SISNAFTAHP CDSVSQTMCD GDSCGGTYSA SGDRYSGTCD PDGCDYNPYR LGNTDFYGPG 310 320 330 340 350 360 LTVDTNSPFT VVTQFITDDG TSSGTLTEIK RLYVQNGEVI ANGASTYSSV NGSSITSAFC 370 380 390 400 410 420 ESEKTLFGDE NVFDKHGGLE GMGEAMAKGM VLVLSLWDDY AADMLWLDSD YPVNSSASTP 430 440 450 460 470 480 GVARGTCSTD SGVPATVEAE SPNAYVTYSN IKFGPIGSTY SSGSSSGSGS SSSSSSTTTK 490 500 510 520 530 ATSTTLKTTS TTSSGSSSTS AAQAYGQCGG QGWTGPTTCV SGYTCTYENA YYSQCL

References

[1]	"Two cellobiohydrolase-encoding genes from Aspergillus niger require D-xylose and the xylanolytic transcriptional activator XlnR for their expression." Gielkens M.M., Dekkers E., Visser J., de Graaff L.H. Appl. Environ. Microbiol. 65:4340-4345(1999) [PubMed: 10508057] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION. Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
[2]	"Induction, production, repression, and de-repression of exoglucanase synthesis in Aspergillus niger." Hanif A., Yasmeen A., Rajoka M.I. Bioresour. Technol. 94:311-319(2004) [PubMed: 15182839] [Abstract] Cited for: FUNCTION, INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF156269 Genomic DNA. Translation: AAF04492.1.
3D structure databases
HSSP	HSSP built from PDB template 1GPI based on UniProtKB Q09431.
ProteinModelPortal	Q9UVS8.
SMR	Q9UVS8. Positions 22-461, 502-536.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9UVS8.
Protein family/group databases
CAZy	CBM1. Carbohydrate-Binding Module Family 1. GH7. Glycoside Hydrolase Family 7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR000254. Cellulose-bd_dom_fun. IPR008985. ConA-like_lec_gl. 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_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

CBHB_ASPNG

Accession

Primary (citable) accession number: Q9UVS8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 20, 2010
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program