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A2QL72

- AGALA_ASPNC

UniProt

A2QL72 - AGALA_ASPNC

Protein

Probable alpha-galactosidase A

Gene

aglA

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 44 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides.By similarity

    Catalytic activityi

    Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei154 – 1541NucleophileBy similarity
    Active sitei212 – 2121Proton donorBy similarity

    GO - Molecular functioni

    1. galactosidase activity Source: ASPGD
    2. hydrolase activity, acting on glycosyl bonds Source: ASPGD
    3. raffinose alpha-galactosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    Lectin

    Protein family/group databases

    CAZyiCBM13. Carbohydrate-Binding Module Family 13.
    GH27. Glycoside Hydrolase Family 27.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable alpha-galactosidase A (EC:3.2.1.22)
    Alternative name(s):
    Melibiase A
    Gene namesi
    Name:aglA
    ORF Names:An06g00170
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 8ER

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 537514Probable alpha-galactosidase APRO_5000220032Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi46 ↔ 78PROSITE-ProRule annotation
    Glycosylationi49 – 491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi87 – 871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi123 – 1231N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi126 ↔ 156PROSITE-ProRule annotation
    Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi355 – 3551N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi430 ↔ 444PROSITE-ProRule annotation
    Glycosylationi436 – 4361N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi469 ↔ 482PROSITE-ProRule annotation
    Glycosylationi491 – 4911N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00004923.

    Structurei

    3D structure databases

    ProteinModelPortaliA2QL72.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini413 – 537125Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 27 family.Curated
    Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000161224.
    KOiK07407.
    OrthoDBiEOG7SR4WK.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR013780. Glyco_hydro_13_b.
    IPR002241. Glyco_hydro_27.
    IPR000111. Glyco_hydro_GHD.
    IPR017853. Glycoside_hydrolase_SF.
    IPR000772. Ricin_B_lectin.
    [Graphical view]
    PfamiPF02065. Melibiase. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view]
    PRINTSiPR00740. GLHYDRLASE27.
    SMARTiSM00458. RICIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF50370. SSF50370. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS00512. ALPHA_GALACTOSIDASE. 1 hit.
    PS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    A2QL72-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNQGTKSILL AATLAAIPWQ VYGSIEQSSL LPIPPMGFNN WARFMCDLNE    50
    TLFTETADAM AANGLRDAGY NRINLDDCWM AYQRSDNGSL QWNTTKFPHG 100
    LPWLAQYVKA KGFHFGIYED SGNMTCGGYP GSYNHEEQDA NTFALWGIDY 150
    LKLDGCNVYA TQGRTLEEEY KQRYGHWHQV LSKMQHPLIF SESAPAYFAG 200
    TDNNTDWYTV MDWVPIYGEL ARHSTDILVY SGAGSAWDSI MNNYNYNTLL 250
    ARYQRPGYFN DPDFLIPDHP GLTADEKRSH FALWASFSAP LIISAYIPAL 300
    SKDEIAFLTN EALIAVNQDP LAQQATFASR DNTLDILTRN LANGDRLLTV 350
    LNKGNTTVTR DIPVQWLGLT ETDCTYTAED LWDGKTQKIS DHIKIELASH 400
    ATAVFRLGLP QGCSSVVPTG LVFNTASGNC LTAASNSSVA FQSCNGETSQ 450
    IWQVTLSGVI RPVSQTTQCL AADGNSVKLQ ACDSTDSDGQ NWTYAVTGNL 500
    KNAKTDGCLT EGSVQMKSCL YERDGQVFGL PSGVQLS 537
    Length:537
    Mass (Da):59,213
    Last modified:March 6, 2007 - v1
    Checksum:iF093FD8196C7F839
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270108 Genomic DNA. Translation: CAK44933.1.
    RefSeqiXP_001390845.1. XM_001390808.1.

    Genome annotation databases

    EnsemblFungiiCADANGAT00005022; CADANGAP00004923; CADANGAG00005022.
    GeneIDi4981013.
    KEGGiang:ANI_1_6054.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270108 Genomic DNA. Translation: CAK44933.1 .
    RefSeqi XP_001390845.1. XM_001390808.1.

    3D structure databases

    ProteinModelPortali A2QL72.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00004923.

    Protein family/group databases

    CAZyi CBM13. Carbohydrate-Binding Module Family 13.
    GH27. Glycoside Hydrolase Family 27.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00005022 ; CADANGAP00004923 ; CADANGAG00005022 .
    GeneIDi 4981013.
    KEGGi ang:ANI_1_6054.

    Phylogenomic databases

    HOGENOMi HOG000161224.
    KOi K07407.
    OrthoDBi EOG7SR4WK.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR013780. Glyco_hydro_13_b.
    IPR002241. Glyco_hydro_27.
    IPR000111. Glyco_hydro_GHD.
    IPR017853. Glycoside_hydrolase_SF.
    IPR000772. Ricin_B_lectin.
    [Graphical view ]
    Pfami PF02065. Melibiase. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view ]
    PRINTSi PR00740. GLHYDRLASE27.
    SMARTi SM00458. RICIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50370. SSF50370. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS00512. ALPHA_GALACTOSIDASE. 1 hit.
    PS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view ]
    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 nameiAGALA_ASPNC
    AccessioniPrimary (citable) accession number: A2QL72
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 23, 2010
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 44 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