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A2QN74

- BTGC_ASPNC

UniProt

A2QN74 - BTGC_ASPNC

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Protein

Putative glucan endo-1,3-beta-glucosidase btgC

Gene
btgC, An07g04650
Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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 By similarity.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei586 – 5861Nucleophile By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. polysaccharide catabolic process Source: UniProtKB-KW
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.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative 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:An07g04650
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 4L

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 302302Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei303 – 32321Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini324 – 684361Extracellular Reviewed predictionAdd
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 – 684684Putative glucan endo-1,3-beta-glucosidase btgCPRO_0000395125Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi404 – 4041N-linked (GlcNAc...) Reviewed prediction
Glycosylationi427 – 4271N-linked (GlcNAc...) Reviewed prediction
Glycosylationi455 – 4551N-linked (GlcNAc...) Reviewed prediction
Glycosylationi474 – 4741N-linked (GlcNAc...) Reviewed prediction
Glycosylationi631 – 6311N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi245 – 358114Gly-richAdd
BLAST
Compositional biasi337 – 34610Poly-Ser

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5309.
HOGENOMiHOG000173877.
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.

A2QN74-1 [UniParc]FASTAAdd to Basket

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MAGVNRSFSY SRGDDALLRD DEREISPLRS AEDGLYSTSY GDVSPLSAGV    50
QAQNRPFDRG LVSVPEGQTL ERHMTSTPGM DNLGPASVGG GISGIALGVA 100
NSHNRQSGVD AFRETDVPVR NLPAERDFNT TGSDNPYIPA PPDGDIYPSS 150
EAVRYRDSYS SHTGLGAGAP FAEHSTPGTT PSQRSFFDSP YQGVDAGPYQ 200
RHSAYSSHDY PLVINPDDIA DDGDDGFPVH PKGAADYRSN ANVPGTGVAG 250
AAAAGGFLGK FRALFKREEP SPFYDSDIGG GLGGAEKAQG GRHIIGGGSR 300
KRGWIVGLIL AAVIVAAIVG GAVGGILGHQ EHDGDTSSSS SSSSSSGTGS 350
GGSDKGDGLL DKDSDEIKAL MNNKNLHKVF PGVDYTPWGV QYPLCLQYPP 400
SQNNVTRDLA VLTQLTNTIR LYGTDCNQTE MVLEAIDRLQ LTNMKLWLGV 450
WIDTNTTTTD RQISQLYKIV ENANDTSIFK GAIVGNEALY RAGSDVASAE 500
TNLIGYINDV KDHFKDKNID LPVGTSDLGD NWNAQLVSAA DFVMSNIHPF 550
FGGVEIDDAA SWTWTFWQTH DTPLTAGTNK QQIISEVGWP TGGGNDCGSD 600
NKCQNDKQGA VAGIDELNQF LSEWVCQALD NGTEYFWFEA FDEPWKVQYN 650
TPGQEWEDKW GLMDSARNLK PGVKIPDCGG KTIT 684
Length:684
Mass (Da):73,248
Last modified:June 15, 2010 - v2
Checksum:i5CB65C56222424D0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270130 Genomic DNA. Translation: CAK39383.1.
RefSeqiXP_001391547.2. XM_001391510.2.

Genome annotation databases

GeneIDi4981731.
KEGGiang:ANI_1_1742064.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270130 Genomic DNA. Translation: CAK39383.1 .
RefSeqi XP_001391547.2. XM_001391510.2.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 4981731.
KEGGi ang:ANI_1_1742064.

Phylogenomic databases

eggNOGi COG5309.
HOGENOMi HOG000173877.
OrthoDBi EOG7P8PHC.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiBTGC_ASPNC
AccessioniPrimary (citable) accession number: A2QN74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: February 19, 2014
This is version 39 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

Lacks the conserved Glu residue in position 619 essential for glucanase activity. Its enzyme activity is therefore unsure.

Keywords - Technical termi

Complete 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

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