Q5BDU5 (EGLA_EMENI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Carboxymethylcellulase A
Cellulase A

Gene names

Name:	eglA
ORF Names:	AN1285

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	326 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 Ref.2
Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Subcellular location	Secreted By similarity.
Induction	Highly expressed in presence of carboxymethylcellulose (CMC). Ref.1
Sequence similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) family.
Biophysicochemical properties	pH dependence: Optimum pH is 4.0. Ref.2 Temperature dependence: Optimum temperature is 57 degrees Celsius.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
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.2. Source: UniProtKB
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cellulase activity Inferred from direct assay Ref.2. Source: UniProtKB
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 – 326	307	Endo-beta-1,4-glucanase A		PRO_5000049150
Sites
	Active site	150	1	Proton donor By similarity
	Active site	257	1	Nucleophile By similarity
Experimental info
	Sequence conflict	116	1	Missing in BAA82592. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q5BDU5 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: 7BFED0EF254B8D9F	FASTA	326	35,812
	10 20 30 40 50 60 MRSLVLLSSV LALVAPSKGA FTWLGTNEAG AEFGEGSYPG ELGTEYIWPD LGTIGTLRNE 70 80 90 100 110 120 GMNIFRVAFS MERLVPDSLA GPVADEYFQD LVETVNGITA LGAYAVLDPH NYGRYYGNII 130 140 150 160 170 180 TSTDDFAAFW TILATEFASN ELVIFDTNNE YHTMDQSLVL NLNQAAIDAI RASGATSQYI 190 200 210 220 230 240 FAEGNSWTGA WTWVDVNDNM KALTDPQDKL IYEMHQYLDS DGSGTNTACV SSTIGSERVT 250 260 270 280 290 300 AATNWLRENG KLGVLGEFAG ANNQVCKDAV ADLLEYLEEN SDVWLGALWW AAGPWWGDYM 310 320 FNMEPTSGIA YQEYSEILQP YFVGSQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression properties of the endo-beta-1,4-glucanase A gene from the filamentous fungus Aspergillus nidulans." Chikamatsu G., Shirai K., Kato M., Kobayashi T., Tsukagoshi N. FEMS Microbiol. Lett. 175:239-245(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, 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	AB009402 Genomic DNA. Translation: BAA82592.1. DQ490472 mRNA. Translation: ABF50848.1. AACD01000017 Genomic DNA. Translation: EAA65878.1. BN001308 Genomic DNA. Translation: CBF87793.1.
RefSeq	XP_658889.1. XM_653797.1.
3D structure databases
ProteinModelPortal	Q5BDU5.
SMR	Q5BDU5. Positions 21-322.
ModBase	Search...
Protein family/group databases
mycoCLAP	EGL5A_EMENI. EGL5B_EMENI.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00001335; CADANIAP00001335; CADANIAG00001335.
GeneID	2877061.
KEGG	ani:AN1285.2.
Phylogenomic databases
eggNOG	COG2730.
HOGENOM	HOG000111120.
KO	K01179.
OMA	GSDKPQM.
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

EGLA_EMENI

Accession

Primary (citable) accession number: Q5BDU5
Secondary accession number(s): C8VSF3, Q1HFV2, Q9Y8H6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 18, 2010
Last sequence update:	April 26, 2005
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program