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Q2UIE6

- EGLX_ASPOR

UniProt

Q2UIE6 - EGLX_ASPOR

Protein

Probable endo-1,3(4)-beta-glucanase AO090023000083

Gene

AO090023000083

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (24 Jan 2006)
      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 sitei144 – 1441NucleophileBy similarity
    Active sitei149 – 1491Proton 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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable endo-1,3(4)-beta-glucanase AO090023000083 (EC:3.2.1.6)
    Alternative name(s):
    Mixed-linked glucanase AO090023000083
    Gene namesi
    ORF Names:AO090023000083
    OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
    Taxonomic identifieri510516 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006564: Chromosome 3

    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 – 643619Probable endo-1,3(4)-beta-glucanase AO090023000083PRO_0000395091Add
    BLAST
    Propeptidei644 – 66724Removed in mature formSequence AnalysisPRO_0000395092Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
    Lipidationi643 – 6431GPI-anchor amidated alanineSequence Analysis

    Keywords - PTMi

    Glycoprotein, GPI-anchor, Lipoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ2UIE6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi583 – 61533Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 16 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000166269.
    OMAiSCVNYVA.
    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.

    Q2UIE6-1 [UniParc]FASTAAdd to Basket

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    MSSSSFVWTV GSIALSSLIT PTIADGSGSR YQLTEAWQGE KFLDHFKFFS    50
    GSDPTNGFVT YANQSYAESS GLIEVTESGS FYMGVDYKTK LSPNGPGRDS 100
    VRIESKEYYD EGLYIIDLQH MPGSVCGTWP AFWSVGPNWP YDGEIDIIEG 150
    VNKHEANEIV LHTSGSCSLS SENDMSGTMT SSECGESSGT IGCVVKGQDG 200
    TSGAPFNEKN GGVYAMEWTS SFVKIWYFAR SEIPQSITEG NPDTTAFGTP 250
    MAHLQGTCDF GERFKSQKFI LDTTFCGDWA GGVFGDSGCP VSDPSNPIQS 300
    CVNYVAENPA AFKEAYWEIN YIKLFQTGTG HSTASVASQA ETATAVASNT 350
    VDSIPSVTST AIPETTAPAP ETVSAEAPAT SSAVPEPANP QTSVAGAETT 400
    AAPAPSPETT AAPASPSLDD SDGADAVSET TIYVTETTTI CGASTQKGTI 450
    QTIGGGETEV SPASSTVESA ATPAAPTPTS QKPVASLPGT TVNGGTPVPT 500
    DVSPETPAEE TAGESGAPTP SAEQPEQPQP AATSIETGTV PPAVSNPAPT 550
    EQGTPEGASP VDATESRHDS DEPAPTSAAP IRSPSPSSWT ISSSSRVASS 600
    SSFASTTSSA SRTTSATKEA TAPTETDSGA STGTNPESPV FTAGASKSVG 650
    ISGLTGIVCG IAMAMLA 667
    Length:667
    Mass (Da):68,301
    Last modified:January 24, 2006 - v1
    Checksum:iA37D2DC90AF23769
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP007157 Genomic DNA. Translation: BAE58669.1.
    RefSeqiXP_001820671.1. XM_001820619.1.

    Genome annotation databases

    EnsemblFungiiCADAORAT00007233; CADAORAP00007095; CADAORAG00007233.
    GeneIDi5992673.
    KEGGiaor:AOR_1_1840144.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP007157 Genomic DNA. Translation: BAE58669.1 .
    RefSeqi XP_001820671.1. XM_001820619.1.

    3D structure databases

    ProteinModelPortali Q2UIE6.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAORAT00007233 ; CADAORAP00007095 ; CADAORAG00007233 .
    GeneIDi 5992673.
    KEGGi aor:AOR_1_1840144.

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000166269.
    OMAi SCVNYVA.
    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 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 nameiEGLX_ASPOR
    AccessioniPrimary (citable) accession number: Q2UIE6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 49 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