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Protein

Glucan endo-1,3-beta-glucosidase btgC

Gene

btgC

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

Functioni

Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation. Active on laminarin and lichenan.1 Publication

Catalytic activityi

Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei551 – 5511NucleophileBy similarity
Active sitei619 – 6191Proton donorBy similarity

GO - Molecular functioni

  1. glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. glucan catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.
mycoCLAPiLAM17A_EMENI.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan endo-1,3-beta-glucosidase btgC (EC:3.2.1.39)
Alternative name(s):
Endo-1,3-beta-glucanase btgC
Laminarinase btgC
Gene namesi
Name:btgC
ORF Names:AN4700
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome III

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 274274CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei275 – 29521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini296 – 649354ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 649649Glucan endo-1,3-beta-glucosidase btgCPRO_0000395128Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi369 – 3691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi392 – 3921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi420 – 4201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi596 – 5961N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5B430.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi222 – 30079Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 17 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5309.
HOGENOMiHOG000173877.
InParanoidiQ5B430.
OMAiSDNPYVP.
OrthoDBiEOG7P8PHC.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5B430-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDRSEQYGD IPPISSQHRM HGYGNNGEPA AMPGDGQQNW GSGPGIAHTH
60 70 80 90 100
SMRTASTATP GMDNLGPSAV GGGISGIALG VANTHDRQSG IDAFRDADAT
110 120 130 140 150
LGYIPAERGY HTTGADNPYV PSPPSVGPGP DESSEGLRSH ETFGSSAALS
160 170 180 190 200
AAGAPAGNWT PPSGSRHSFL DGSYQGVASG PYQRHSAYSS QDYPADINPD
210 220 230 240 250
DILDDGDDGF AAAPSNKPNA AGGAATGGAA GGLLGEFFGA KKAADASYDP
260 270 280 290 300
VPGAGLPSVE KYAKPRPSGA SRKRGWIIGG ILAFIVIGAI VGGAVGGTLG
310 320 330 340 350
NRRSETASES SEVSADDDTE TNGDLDKNSD EIKSLMAMEG LHKVFPGMDY
360 370 380 390 400
TPWGVQHPEC DKWPPSQNNV TRDMAVLSRL TNTVRLYGTD CNQTEMVLHA
410 420 430 440 450
IDRLELTDMK LWLGVWIDTN TTTNERQLSQ LYDILDKRSD HSVFKGAIIG
460 470 480 490 500
NEALYRAGST KEEARKNIID YMRQVRKHFN DHNIDIKVAT SDLGDNWDET
510 520 530 540 550
LADATDVVMS NVHPFFGGVE VSKAAGWTWS FWNSHNAPLT QGTNKGNIIA
560 570 580 590 600
EVGWPSGGGN DCGDGANCKD DTSGAVAGVK QMNQFMADWV CPALENGTDY
610 620 630 640
FWFEAFDEPW KVKFNKGDEQ WEDKWGLMDP GRNLKPGIEI PDCGGKTAA
Length:649
Mass (Da):68,963
Last modified:April 26, 2005 - v1
Checksum:i8476F1DF5B3F1D93
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490493 mRNA. Translation: ABF50869.1.
AACD01000080 Genomic DNA. Translation: EAA60742.1.
BN001303 Genomic DNA. Translation: CBF76969.1.
RefSeqiXP_662304.1. XM_657212.1.

Genome annotation databases

EnsemblFungiiCADANIAT00005730; CADANIAP00005730; CADANIAG00005730.
GeneIDi2872500.
KEGGiani:AN4700.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490493 mRNA. Translation: ABF50869.1.
AACD01000080 Genomic DNA. Translation: EAA60742.1.
BN001303 Genomic DNA. Translation: CBF76969.1.
RefSeqiXP_662304.1. XM_657212.1.

3D structure databases

ProteinModelPortaliQ5B430.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.
mycoCLAPiLAM17A_EMENI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00005730; CADANIAP00005730; CADANIAG00005730.
GeneIDi2872500.
KEGGiani:AN4700.2.

Phylogenomic databases

eggNOGiCOG5309.
HOGENOMiHOG000173877.
InParanoidiQ5B430.
OMAiSDNPYVP.
OrthoDBiEOG7P8PHC.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  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.

Entry informationi

Entry nameiBTGC_EMENI
AccessioniPrimary (citable) accession number: Q5B430
Secondary accession number(s): C8VAX6, Q1HFT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: January 7, 2015
This is version 57 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.