Q8NK02 (CBHB_EMENI) 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
ORF Names:	AN0494

Organism

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

Taxonomic identifier

227321 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	526 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. Ref.4
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.
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
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 direct assay. 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 – 23	23	Potential
	Chain	24 – 526	503	1,4-beta-D-glucan cellobiohydrolase B		PRO_0000393550
Regions
	Domain	490 – 526	37	CBM1
	Region	24 – 458	435	Catalytic
	Region	459 – 490	32	Ser/Thr-rich linker
Sites
	Active site	235	1	Nucleophile By similarity
	Active site	240	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	293	1	N-linked (GlcNAc...) Potential
	Glycosylation	400	1	N-linked (GlcNAc...) Potential
	Disulfide bond	498 ↔ 515		By similarity
	Disulfide bond	509 ↔ 525		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8NK02 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 9A9CD7C5BEBCB6C9	FASTA	526	56,123
	10 20 30 40 50 60 MASSFQLYKA LLFFSSLLSA VQAQKVGTQQ AEVHPGLTWQ TCTSSGSCTT VNGEVTIDAN 70 80 90 100 110 120 WRWLHTVNGY TNCYTGNEWD TSICTSNEVC AEQCAVDGAN YASTYGITTS GSSLRLNFVT 130 140 150 160 170 180 QSQQKNIGSR VYLMDDEDTY TMFYLLNKEF TFDVDVSELP CGLNGAVYFV SMDADGGKSR 190 200 210 220 230 240 YATNEAGAKY GTGYCDSQCP RDLKFINGVA NVEGWESSDT NPNGGVGNHG SCCAEMDIWE 250 260 270 280 290 300 ANSISTAFTP HPCDTPGQTL CTGDSCGGTY SNDRYGGTCD PDGCDFNSYR QGNKTFYGPG 310 320 330 340 350 360 LTVDTNSPVT VVTQFLTDDN TDTGTLSEIK RFYVQNGVVI PNSESTYPAN PGNSITTEFC 370 380 390 400 410 420 ESQKELFGDV DVFSAHGGMA GMGAALEQGM VLVLSLWDDN YSNMLWLDSN YPTDADPTQP 430 440 450 460 470 480 GIARGTCPTD SGVPSEVEAQ YPNAYVVYSN IKFGPIGSTF GNGGGSGPTT TVTTSTATST 490 500 510 520 TSSATSTATG QAQHWEQCGG NGWTGPTVCA SPWACTVVNS WYSQCL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Regulation by carbon and nitrogen sources of a family of cellulases in Aspergillus nidulans." Lockington R.A., Rodbourn L., Barnett S., Carter C.J., Kelly J.M. Fungal Genet. Biol. 37:190-196(2002) [PubMed: 12409103] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 16372000] [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: 19146970] [Abstract] Cited for: GENOME REANNOTATION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[4]	"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: 16844780] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF420020 Genomic DNA. Translation: AAM54070.1. AACD01000007 Genomic DNA. Translation: EAA66593.1. BN001308 Genomic DNA. Translation: CBF89371.1.
RefSeq	XP_658098.1. XM_653006.1.
3D structure databases
HSSP	HSSP built from PDB template 1GPI based on UniProtKB Q09431.
ProteinModelPortal	Q8NK02.
SMR	Q8NK02. Positions 24-460, 492-526.
ModBase	Search...
Protein family/group databases
CAZy	CBM1. Carbohydrate-Binding Module Family 1. GH7. Glycoside Hydrolase Family 7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00002195; CADANIAP00002195; CADANIAG00002195.
GeneID	2876273.
KEGG	ani:AN0494.2.
Phylogenomic databases
OMA	GSCCAEM.
OrthoDB	EOG4K3Q4P.
PhylomeDB	Q8NK02.
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_EMENI

Accession

Primary (citable) accession number: Q8NK02
Secondary accession number(s): C8VSY4, Q5BG36

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 20, 2010
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program