Q1HFS8 (EGLB_EMENI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endo-beta-1,4-glucanase B
Short name=Endoglucanase B
EC=3.2.1.4

Alternative name(s):
Carboxymethylcellulase B
Cellulase B

Gene names

Name:	eglB
ORF Names:	AN5214

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	328 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	Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates. Ref.1
Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) family.
Biophysicochemical properties	pH dependence: Optimum pH is 4.0. Ref.1 Temperature dependence: Optimum temperature is 52 degrees Celsius.
Sequence caution	The sequence CBF81096.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAA62395.1 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	Glycoprotein
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 Ref.1. Source: UniProtKB
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cellulase activity Inferred from direct assay Ref.1. Source: UniProtKB
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 – 328	311	Endo-beta-1,4-glucanase B		PRO_0000394058
Sites
	Active site	155	1	Proton donor By similarity
	Active site	262	1	Nucleophile By similarity
Amino acid modifications
	Glycosylation	95	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q1HFS8 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: 7FBF3D7078476B4D	FASTA	328	36,080
	10 20 30 40 50 60 MKVNTLLVAV AAGTAMAAPQ LKKRAGFTFF GVTEAGAEFG EKSIPGVWGT DYTFPDTESI 70 80 90 100 110 120 LTLISKGFNT FRIPFLMERL TPEMTGSFDE GYLKNLTSVV NAVTDAGAWA IVDAQNFGRF 130 140 150 160 170 180 NGEIISSASD FQTWWKNVAA EFADNKNVIF DTNNEFHDMD QTLVLDLNQA AINGIRAAGA 190 200 210 220 230 240 TSQYIFVEGN SYTGAWTWTD NNDNLKSLTD PQDKIVYEMH QYLDTDGSGT HETCVSETIG 250 260 270 280 290 300 AERVESATQW LKDNGKLGVI GEFAGGNNEI CRAAVKSLLD ALKENDDVWL GALWWAAGPW 310 320 WEDYMFSMEP TDGIAYTGML STLEAYMN

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	DQ490496 mRNA. Translation: ABF50872.1. AACD01000089 Genomic DNA. Translation: EAA62395.1. Sequence problems. BN001305 Genomic DNA. Translation: CBF81096.1. Sequence problems.
RefSeq	XP_662818.1. XM_657726.1.
3D structure databases
ProteinModelPortal	Q1HFS8.
SMR	Q1HFS8. Positions 27-327.
ModBase	Search...
Protein family/group databases
mycoCLAP	EGL5C_EMENI.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2871506.
KEGG	ani:AN5214.2.
Phylogenomic databases
eggNOG	COG2730.
HOGENOM	HOG000111120.
KO	K01179.
OrthoDB	EOG43NBNF.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR001547. Glyco_hydro_5. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF00150. Cellulase. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

EGLB_EMENI

Accession

Primary (citable) accession number: Q1HFS8
Secondary accession number(s): C8VF90, Q5B2L6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 18, 2010
Last sequence update:	June 13, 2006
Last modified:	May 1, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program