Q4WFK4 (CBHC_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:	cbhC
ORF Names:	AFUA_3G01910

Organism

Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]

Taxonomic identifier

330879 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Neosartorya fumigata

Protein attributes

Sequence length	454 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 By similarity.
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 By similarity.
Domain	Has a modular structure: a carbohydrate-binding module (CBM) at the N-terminus, a linker rich in threonines, and a C-terminal exocellobiohydrolase catalytic module. The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Sequence similarities	Belongs to the glycosyl hydrolase 6 (cellulase B) 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
Technical term	Complete proteome Reference proteome
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 – 19	19	Potential
	Chain	20 – 454	435	Probable 1,4-beta-D-glucan cellobiohydrolase C		PRO_0000394051
Regions
	Domain	20 – 55	36	CBM1
	Region	59 – 94	36	Thr-rich linker
	Region	95 – 454	360	Catalytic
Sites
	Active site	184	1	By similarity
	Active site	230	1	Proton donor By similarity
	Active site	409	1	Nucleophile By similarity
Amino acid modifications
	Glycosylation	413	1	N-linked (GlcNAc...) Potential
	Disulfide bond	27 ↔ 44		By similarity
	Disulfide bond	38 ↔ 54		By similarity
	Disulfide bond	185 ↔ 244		By similarity
	Disulfide bond	376 ↔ 423		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4WFK4 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: 9EFFB0212288A576	FASTA	454	47,796
	10 20 30 40 50 60 MKHLASSIAL TLLLPAVQAQ QTVWGQCGGQ GWSGPTSCVA GAACSTLNPY YAQCIPGATA 70 80 90 100 110 120 TSTTLTTTTA ATTTSQTTTK PTTTGPTTSA PTVTASGNPF SGYQLYANPY YSSEVHTLAM 130 140 150 160 170 180 PSLPSSLQPK ASAVAEVPSF VWLDVAAKVP TMGTYLADIQ AKNKAGANPP IAGIFVVYDL 190 200 210 220 230 240 PDRDCAALAS NGEYSIANNG VANYKAYIDA IRAQLVKYSD VHTILVIEPD SLANLVTNLN 250 260 270 280 290 300 VAKCANAQSA YLECVDYALK QLNLPNVAMY LDAGHAGWLG WPANLGPAAT LFAKVYTDAG 310 320 330 340 350 360 SPAAVRGLAT NVANYNAWSL STCPSYTQGD PNCDEKKYIN AMAPLLKEAG FDAHFIMDTS 370 380 390 400 410 420 RNGVQPTKQN AWGDWCNVIG TGFGVRPSTN TGDPLQDAFV WIKPGGESDG TSNSTSPRYD 430 440 450 AHCGYSDALQ PAPEAGTWFQ AYFEQLLTNA NPSF

References

[1]

"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAHF01000010 Genomic DNA. Translation: EAL86473.1.
RefSeq	XP_748511.1. XM_743418.1.
3D structure databases
ProteinModelPortal	Q4WFK4.
SMR	Q4WFK4. Positions 21-55, 92-454.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUAT00000253; CADAFUAP00000253; CADAFUAG00000253.
GeneID	3505986.
KEGG	afm:AFUA_3G01910.
Phylogenomic databases
eggNOG	COG5297.
HOGENOM	HOG000178851.
KO	K01238.
OMA	KAGANPP.
OrthoDB	EOG4WDHM5.
Family and domain databases
Gene3D	3.20.20.40. 1 hit.
InterPro	IPR016288. Beta_cellobiohydrolase. IPR000254. Cellulose-bd_dom_fun. IPR001524. Glyco_hydro_6_CS. [Graphical view]
Pfam	PF00734. CBM_1. 1 hit. PF01341. Glyco_hydro_6. 1 hit. [Graphical view]
PIRSF	PIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTS	PR00733. GLHYDRLASE6.
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. SSF51989. Glyco_hydro_6. 1 hit.
PROSITE	PS00562. CBM1_1. 1 hit. PS51164. CBM1_2. 1 hit. PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit. PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CBHC_ASPFU

Accession

Primary (citable) accession number: Q4WFK4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 18, 2010
Last sequence update:	July 5, 2005
Last modified:	May 1, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program