Q5B2Q4 (CBHA_EMENI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Beta-glucancellobiohydrolase A
Cellobiohydrolase D
Exocellobiohydrolase A
Exoglucanase A

Gene names

Name:	cbhA
Synonyms:	celD
ORF Names:	AN5176

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	446 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	Repressed by D-glucose. Ref.1
Sequence similarities	Belongs to the glycosyl hydrolase 7 (cellulase C) family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Chain	18 – 446	429	Probable 1,4-beta-D-glucan cellobiohydrolase A		PRO_0000393544
Sites
	Active site	226	1	Nucleophile By similarity
	Active site	231	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	81	1	N-linked (GlcNAc...) Potential
	Glycosylation	284	1	N-linked (GlcNAc...) Potential
	Glycosylation	333	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	150	1	L → F in AAM54069. Ref.1
	Sequence conflict	286	1	S → R in AAM54069. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q5B2Q4 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: DACEE446E809A6D2	FASTA	446	47,638
	10 20 30 40 50 60 MYQRALLFSA LLSVSRAQQA GTAQEEVHPS LTWQRCEASG SCTEVAGSVV LDSNWRWTHS 70 80 90 100 110 120 VDGYTNCYTG NEWDATLCPD NESCAQNCAV DGADYEATYG ITSNGDSLTL KFVTGSNVGS 130 140 150 160 170 180 RVYLMEDDET YQMFDLLNNE FTFDVDVSNL PCGLNGALYF TSMDADGGLS KYEGNTAGAK 190 200 210 220 230 240 YGTGYCDSQC PRDIKFINGL GNVEGWEPSD SDANAGVGGM GTCCPEMDIW EANSISTAYT 250 260 270 280 290 300 PHPCDSVEQT MCEGDSCGGT YSDDRYGGTC DPDGCDFNSY RMGNTSFYGP GAIIDTSSKF 310 320 330 340 350 360 TVVTQFIADG GSLSEIKRFY VQNGEVIPNS ESNISGVEGN SITSEFCTAQ KTAFGDEDIF 370 380 390 400 410 420 AQHGGLSAMG DAASAMVLIL SIWDDHHSSM MWLDSSYPTD ADPSQPGVAR GTCEQGAGDP 430 440 DVVESEHADA SVTFSNIKFG PIGSTF

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
[2]	"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.
[3]	"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.
[4]	"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	AF420019 Genomic DNA. Translation: AAM54069.1. DQ490495 mRNA. Translation: ABF50871.1. AACD01000089 Genomic DNA. Translation: EAA62357.1. BN001305 Genomic DNA. Translation: CBF81021.1.
RefSeq	XP_662780.1. XM_657688.1.
3D structure databases
HSSP	HSSP built from PDB template 1GPI based on UniProtKB Q09431.
ProteinModelPortal	Q5B2Q4.
SMR	Q5B2Q4. Positions 18-446.
ModBase	Search...
Protein family/group databases
CAZy	GH7. Glycoside Hydrolase Family 7.
mycoCLAP	CBH7A_EMENI.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00003171; CADANIAP00003171; CADANIAG00003171.
GeneID	2871468.
KEGG	ani:AN5176.2.
Phylogenomic databases
eggNOG	NOG85664.
HOGENOM	HOG000182210.
OMA	DNESCAQ.
OrthoDB	EOG4K3Q4P.
Family and domain databases
Gene3D	2.70.100.10. 1 hit.
InterPro	IPR008985. ConA-like_lec_gl_sf. IPR001722. Glyco_hydro_7. [Graphical view]
Pfam	PF00840. Glyco_hydro_7. 1 hit. [Graphical view]
PRINTS	PR00734. GLHYDRLASE7.
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CBHA_EMENI

Accession

Primary (citable) accession number: Q5B2Q4
Secondary accession number(s): C8VF49, Q1HFS9, Q8NK03

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 20, 2010
Last sequence update:	April 26, 2005
Last modified:	April 3, 2013
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