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A2QBQ3

- EGLX_ASPNC

UniProt

A2QBQ3 - EGLX_ASPNC

Protein

Probable endo-1,3(4)-beta-glucanase An02g00850

Gene

An02g00850

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 37 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    Mixed-linked glucanase involved in the degradation of complex natural cellulosic substrates.By similarity

    Catalytic activityi

    Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolyzed is itself substituted at C-3.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei140 – 1401NucleophileBy similarity
    Active sitei145 – 1451Proton donorBy similarity

    GO - Molecular functioni

    1. glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group Source: UniProtKB-EC
    2. glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group Source: UniProtKB-EC

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiGH16. Glycoside Hydrolase Family 16.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable endo-1,3(4)-beta-glucanase An02g00850 (EC:3.2.1.6)
    Alternative name(s):
    Mixed-linked glucanase An02g00850
    Gene namesi
    ORF Names:An02g00850
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 4R

    Subcellular locationi

    Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 717693Probable endo-1,3(4)-beta-glucanase An02g00850PRO_5000219530Add
    BLAST
    Propeptidei718 – 73922Removed in mature formSequence AnalysisPRO_0000395090Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi396 – 3961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi459 – 4591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi482 – 4821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi526 – 5261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi537 – 5371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi569 – 5691N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi581 – 5811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi592 – 5921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi620 – 6201N-linked (GlcNAc...)Sequence Analysis
    Lipidationi717 – 7171GPI-anchor amidated glycineSequence Analysis

    Keywords - PTMi

    Glycoprotein, GPI-anchor, Lipoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliA2QBQ3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi287 – 2926Poly-Ser
    Compositional biasi325 – 686362Ala-richAdd
    BLAST
    Compositional biasi419 – 706288Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 16 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000166269.
    OrthoDBiEOG7HB5KN.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 2 hits.

    Sequencei

    Sequence statusi: Complete.

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

    A2QBQ3-1 [UniParc]FASTAAdd to Basket

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    MPTSTLLWSV GSLALSSMVL PAAASSYELV ETWKGEDFLT AFDFYTGADP    50
    TNGFVTYANQ SYAESTGLVK VNSNGTFYMG VDHTTKLSTN GPGRESVRIG 100
    SNKYYDEGLF IIDLQHMPGS VCGTWPAFWS TGKNWPTDGE IDIIEGVNKN 150
    EANEIVLHTS GTCQVSSQKM SGTLTSTECG EDAGTTGCVV EGTQGSSGTP 200
    FNENGGGVYA MQWTDEFLKF WFFPRGSIPS SITKGDPDVA AFGTPMAHME 250
    GSCSIAEHFK AQQFIFDTTF CGDWAGGVYS TSGCPVSDSS SSFKSCVAYV 300
    AENPTAFAES YWEINYIKIY QTGVAASASA SASHVESAAS VAETISAVRE 350
    GTNSVVATTT AATIAVTSTA DAETATTMAG ATTVAASTET SAADENGSSA 400
    STSTHYVTMT TTICPIAESS SAAAALAGGS SEATEASNSE GSPAAATPSS 450
    VTGASAEANE SESTSAAVTT PSTSTGASAE ANGSESSSAS EAGSVAGATP 500
    SSVSTTGASG EADSSEGASA AATPSNVSST GASAEANGSE DSSASSEAKT 550
    VAPSIPSSVT GASAEANGND SASSNAATAS NVSGASAQAG DNESTPASAG 600
    ANAGSSAAPS SVSGASAEAN GSEGSSSHSS GSQAGAHSYG SVPSSAAAYG 650
    RPAPSSSSHA FATAPSSTGS SRVPTSAAAA NNAAAATQGS SASGSNSGSS 700
    GHGSSSATTP STPVFTGGAN KLTLGASSVL SVLAFALLA 739
    Length:739
    Mass (Da):72,556
    Last modified:March 6, 2007 - v1
    Checksum:i7640750996F31B92
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM269996 Genomic DNA. Translation: CAK96300.1.
    RefSeqiXP_001399223.1. XM_001399186.1.

    Genome annotation databases

    EnsemblFungiiCADANGAT00001593; CADANGAP00001543; CADANGAG00001593.
    GeneIDi4978566.
    KEGGiang:ANI_1_2196024.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM269996 Genomic DNA. Translation: CAK96300.1 .
    RefSeqi XP_001399223.1. XM_001399186.1.

    3D structure databases

    ProteinModelPortali A2QBQ3.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH16. Glycoside Hydrolase Family 16.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00001593 ; CADANGAP00001543 ; CADANGAG00001593 .
    GeneIDi 4978566.
    KEGGi ang:ANI_1_2196024.

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000166269.
    OrthoDBi EOG7HB5KN.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 2 hits.
    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 nameiEGLX_ASPNC
    AccessioniPrimary (citable) accession number: A2QBQ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 37 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