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Q2UPQ4

- EGLB_ASPOR

UniProt

Q2UPQ4 - EGLB_ASPOR

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Protein

Probable endo-beta-1,4-glucanase B

Gene

eglB

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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 (By similarity).By similarity

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei160 – 1601Proton donorBy similarity
Active sitei267 – 2671NucleophileBy similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable endo-beta-1,4-glucanase B (EC:3.2.1.4)
Short name:
Endoglucanase B
Alternative name(s):
Carboxymethylcellulase B
Cellulase B
Gene namesi
Name:eglB
Synonyms:celE
ORF Names:AO090005001553
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564: Chromosome 1

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 333316Probable endo-beta-1,4-glucanase BPRO_0000394057Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi37 – 371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5062.CADAORAP00003359.

Structurei

3D structure databases

ProteinModelPortaliQ2UPQ4.
SMRiQ2UPQ4. Positions 30-332.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000111120.
KOiK01179.
OMAiGKGMNIF.
OrthoDBiEOG776T0S.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q2UPQ4 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKFRNLFFAA VAGSAVAAPL AKEQKKRDSV FQWIGANESG AEFGENNLPG
60 70 80 90 100
VWGTDYIFPD VSAITTLIDK GMNIFRIQFK MERLVPDSMT GAYDEAYLQN
110 120 130 140 150
LTTVVNAVTD AGVHAILDPH NYGRFNGEIM STPSDFQTFW KNLAGQFQSN
160 170 180 190 200
SLVIFDTNNE YHDMDQELVL NLNQAAIDGI REAGATEQYI FVEGNSYTGA
210 220 230 240 250
WTWTDVNDNM KNLEDPQDKI VYQMHQYLDS DGSGTSETCV SGTIGQERVT
260 270 280 290 300
SATQWLKDNK KVGIIGEFAG GNNDQCKTAV KGMLDYLAEN TDVWKGALWW
310 320 330
AAGPWWGDYM YSLEPPNGVA FTGMLDVLQA YLG
Length:333
Mass (Da):36,958
Last modified:January 24, 2006 - v1
Checksum:iEA1271CB19A55C7A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451G → E in BAD72778. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB195229 Genomic DNA. Translation: BAD72778.1.
AP007151 Genomic DNA. Translation: BAE56461.1.
RefSeqiXP_001818463.1. XM_001818411.1.

Genome annotation databases

EnsemblFungiiCADAORAT00003416; CADAORAP00003359; CADAORAG00003416.
GeneIDi5990408.
KEGGiaor:AOR_1_2698174.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB195229 Genomic DNA. Translation: BAD72778.1 .
AP007151 Genomic DNA. Translation: BAE56461.1 .
RefSeqi XP_001818463.1. XM_001818411.1.

3D structure databases

ProteinModelPortali Q2UPQ4.
SMRi Q2UPQ4. Positions 30-332.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5062.CADAORAP00003359.

Protein family/group databases

CAZyi GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAORAT00003416 ; CADAORAP00003359 ; CADAORAG00003416 .
GeneIDi 5990408.
KEGGi aor:AOR_1_2698174.

Phylogenomic databases

eggNOGi COG2730.
HOGENOMi HOG000111120.
KOi K01179.
OMAi GKGMNIF.
OrthoDBi EOG776T0S.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00150. Cellulase. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and overexpression of a novel cellulase gene, celE, from Aspergillus oryzae KBN616."
    Yasuda-Yoshino S., Kitamoto N.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: KBN616.
  2. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiEGLB_ASPOR
AccessioniPrimary (citable) accession number: Q2UPQ4
Secondary accession number(s): Q5TKT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: January 24, 2006
Last modified: October 29, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3