Q5B2E8 (CBHC_EMENI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
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:	AN5282

Organism

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]

Taxonomic identifier

227321 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella › Emericella nidulans › mitosporic Emericella nidulans

Protein attributes

Sequence length	455 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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. Active against carboxymethylcellulose, beta-glucan and lichenan. Ref.1
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.
Biophysicochemical properties	pH dependence: Optimum pH is 5.5. Ref.1 Temperature dependence: Optimum temperature is 57 degrees Celsius.
Sequence caution	The sequence CBF82181.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAA62442.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW glucan catabolic process Inferred from direct assay PubMed 1684480. Source: UniProtKB
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cellulose 1,4-beta-cellobiosidase activity Inferred from direct assay PubMed 1684480. Source: UniProtKB 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 – 455	436	1,4-beta-D-glucan cellobiohydrolase C		PRO_0000394053
Regions
	Domain	20 – 55	36	CBM1
	Region	59 – 92	34	Thr-rich linker
	Region	93 – 450	358	Catalytic
Sites
	Active site	185	1	By similarity
	Active site	231	1	Proton donor By similarity
	Active site	410	1	Nucleophile By similarity
Amino acid modifications
	Disulfide bond	27 ↔ 44		By similarity
	Disulfide bond	38 ↔ 54		By similarity
	Disulfide bond	186 ↔ 245		By similarity
	Disulfide bond	377 ↔ 424		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5B2E8 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 32C2655B3E4CCA1F	FASTA	455	47,624
	10 20 30 40 50 60 MHYSASGLAL AFLLPAIQAQ QTLYGQCGGS GWTGATSCVA GAACSTLNQW YAQCLPAATT 70 80 90 100 110 120 TSTTLTTTTS SVTTTSNPGS TTTTSSVTVT ATASGNPFSG YQLYVNPYYS SEVQSIAIPS 130 140 150 160 170 180 LTGTLSSLAP AATAAAKVPS FVWLDVAAKV PTMATYLADI RSQNAAGANP PIAGQFVVYD 190 200 210 220 230 240 LPDRDCAALA SNGEFAISDG GVQHYKDYID SIREILVEYS DVHVILVIEP DSLANLVTNL 250 260 270 280 290 300 NVAKCANAQS AYLECTNYAV TQLNLPNVAM YLDAGHAGWL GWPANLQPAA NLYAGVYSDA 310 320 330 340 350 360 GSPAALRGLA TNVANYNAWA IDTCPSYTQG NSVCDEKDYI NALAPLLRAQ GFDAHFITDT 370 380 390 400 410 420 GRNGKQPTGQ QAWGDWCNVI GTGFGARPST NTGDSLLDAF VWVKPGGESD GTSDTSAARY 430 440 450 DAHCGYSDAL QPAPEAGTWF QAYFVQLLQN ANPSF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls." Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R. Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]	"The 2008 update of the Aspergillus nidulans genome annotation: a community effort." Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G. Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ490497 mRNA. Translation: ABF50873.1. AACD01000093 Genomic DNA. Translation: EAA62442.1. Sequence problems. BN001305 Genomic DNA. Translation: CBF82181.1. Sequence problems.
RefSeq	XP_662886.1. XM_657794.1.
3D structure databases
ProteinModelPortal	Q5B2E8.
SMR	Q5B2E8. Positions 21-55, 90-455.
ModBase	Search...
Protein family/group databases
mycoCLAP	CBH6C_EMENI.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00003822; CADANIAP00003822; CADANIAG00003822.
GeneID	2871574.
KEGG	ani:AN5282.2.
Phylogenomic databases
eggNOG	COG5297.
HOGENOM	HOG000178851.
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_EMENI

Accession

Primary (citable) accession number: Q5B2E8
Secondary accession number(s): C8VH03, Q1HFS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 18, 2010
Last sequence update:	May 18, 2010
Last modified:	March 6, 2013
This is version 48 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program