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Q5B7R2

- CELB_EMENI

UniProt

Q5B7R2 - CELB_EMENI

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Protein

Endo-beta-1,4-glucanase celB

Gene

celB

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

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.1 Publication

Catalytic activityi

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

pH dependencei

Optimum pH is 5.5.1 Publication

Temperature dependencei

Optimum temperature is 42 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei216 – 2161NucleophileBy similarity
Active sitei221 – 2211Proton donorBy similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH7. Glycoside Hydrolase Family 7.
mycoCLAPiEGL7A_EMENI.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-beta-1,4-glucanase celB (EC:3.2.1.4)
Short name:
Endoglucanase celB
Alternative name(s):
Carboxymethylcellulase celB
Cellulase B
Gene namesi
Name:celB
Synonyms:eglB, eglC
ORF Names:AN3418
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome VI

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 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 430414Endo-beta-1,4-glucanase celBPRO_0000395159Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi43 – 431N-linked (GlcNAc...)Sequence Analysis
Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00009621.

Structurei

3D structure databases

ProteinModelPortaliQ5B7R2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG138370.
HOGENOMiHOG000182210.
InParanoidiQ5B7R2.
OMAiPWINGEA.
OrthoDBiEOG7Q8CXJ.

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5B7R2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALLLSLSLL ATTISAQQIG TPEIRPRLTT YHCTSANGCT EQNTSVVLDA
60 70 80 90 100
ATHPIHDASN PSVSCTTSNG LNPALCPDKQ TCADNCVIDG ITDYAAHGVE
110 120 130 140 150
THGSRLTLTQ YRNVNGALSS VSPRVYLVDE SDPDEQEYRA LSLLAQEFTF
160 170 180 190 200
TVNVSALPCG MNGALYLSEM SPSGGRSALN PAGASYGTGY CDAQCYVNPW
210 220 230 240 250
INGEGNINGY GACCNEMDIW EANSRSTGFT PHACLYEPEE TEGRGVYECA
260 270 280 290 300
SEDECDSAGE NDGICDKWGC GFNPYALGNT EYYGRGQGFE VDTKEPFTVV
310 320 330 340 350
TQFLTDDGTS TGALTEIRRL YIQNGQVIEN AVVSSGADSL TDSLCASTAS
360 370 380 390 400
WFDSYGGMEG MGRALGRGMV LAMSIWNDAG GYMQWLDGGD AGPCNATEGA
410 420 430
PEFIEEHTPW TRVVFEDLKW GDIGSTFQAS
Length:430
Mass (Da):45,929
Last modified:April 26, 2005 - v1
Checksum:i4807FA907F18749E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451S → Y in AAM54071. (PubMed:12409103)Curated
Sequence conflicti73 – 731P → R in AAM54071. (PubMed:12409103)Curated
Sequence conflicti113 – 1131N → Y in AAM54071. (PubMed:12409103)Curated
Sequence conflicti153 – 1531N → Y in AAM54071. (PubMed:12409103)Curated
Sequence conflicti316 – 3161E → D in AAM54071. (PubMed:12409103)Curated
Sequence conflicti345 – 3451C → W in AAM54071. (PubMed:12409103)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF420021 Genomic DNA. Translation: AAM54071.1.
AACD01000055 Genomic DNA. Translation: EAA63386.1.
BN001306 Genomic DNA. Translation: CBF82749.1.
RefSeqiXP_661022.1. XM_655930.1.

Genome annotation databases

EnsemblFungiiCADANIAT00009621; CADANIAP00009621; CADANIAG00009621.
GeneIDi2874128.
KEGGiani:AN3418.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF420021 Genomic DNA. Translation: AAM54071.1 .
AACD01000055 Genomic DNA. Translation: EAA63386.1 .
BN001306 Genomic DNA. Translation: CBF82749.1 .
RefSeqi XP_661022.1. XM_655930.1.

3D structure databases

ProteinModelPortali Q5B7R2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 162425.CADANIAP00009621.

Protein family/group databases

CAZyi GH7. Glycoside Hydrolase Family 7.
mycoCLAPi EGL7A_EMENI.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00009621 ; CADANIAP00009621 ; CADANIAG00009621 .
GeneIDi 2874128.
KEGGi ani:AN3418.2.

Phylogenomic databases

eggNOGi NOG138370.
HOGENOMi HOG000182210.
InParanoidi Q5B7R2.
OMAi PWINGEA.
OrthoDBi EOG7Q8CXJ.

Family and domain databases

Gene3Di 2.70.100.10. 1 hit.
InterProi IPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view ]
Pfami PF00840. Glyco_hydro_7. 1 hit.
[Graphical view ]
PRINTSi PR00734. GLHYDRLASE7.
SUPFAMi SSF49899. SSF49899. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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].
  2. 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.
  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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiCELB_EMENI
AccessioniPrimary (citable) accession number: Q5B7R2
Secondary accession number(s): C8VHK3, Q8NK01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: October 29, 2014
This is version 59 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