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P29064

- AGLU_CANTS

UniProt

P29064 - AGLU_CANTS

Protein

Alpha-glucosidase

Gene
N/A
Organism
Candida tsukubaensis (Yeast) (Pseudozyma tsukubaensis)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
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    Functioni

    Hydrolyzes a broad range of alpha-D-linked glucopyranosides, including maltose (alpha-1,4), sucrose (alpha-1,2), isomaltose (alpha-1,6) and turanose (alpha-1,3).

    Catalytic activityi

    Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei526 – 5261NucleophilePROSITE-ProRule annotation
    Active sitei529 – 5291By similarity
    Active sitei730 – 7301Proton donorBy similarity

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. maltose alpha-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH31. Glycoside Hydrolase Family 31.
    mycoCLAPiAGL31A_CANTS.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-glucosidase (EC:3.2.1.20)
    Alternative name(s):
    Maltase
    Cleaved into the following 2 chains:
    OrganismiCandida tsukubaensis (Yeast) (Pseudozyma tsukubaensis)
    Taxonomic identifieri5483 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaemitosporic UstilaginaceaePseudozyma

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 35351 PublicationAdd
    BLAST
    Chaini36 – 612577Alpha-glucosidase subunit 1PRO_0000018578Add
    BLAST
    Chaini613 – 1070458Alpha-glucosidase subunit 2PRO_0000018579Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi144 – 1441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi208 – 2081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi384 – 3841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi480 – 4801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi513 – 5131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi544 – 5441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi566 – 5661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi574 – 5741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi578 – 5781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi635 – 6351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi818 – 8181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi885 – 8851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi916 – 9161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi983 – 9831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi992 – 9921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi996 – 9961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1008 – 10081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1029 – 10291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1043 – 10431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1052 – 10521N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein, Zymogen

    Structurei

    3D structure databases

    ProteinModelPortaliP29064.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi332 – 3387Poly-Ser

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 31 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF01055. Glyco_hydro_31. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 2 hits.
    SSF74650. SSF74650. 1 hit.
    PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
    PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P29064-1 [UniParc]FASTAAdd to Basket

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    MRSIKAASLT PLLAALFTTL SSTLALPSSV WEHQLETNVL ALRDTNNNGS     50
    SSTISPSFDV TKCPGYKLVG QPQQSQHGFT AQLSLAGDAC NAYGVDIANL 100
    TLSVVYEKQH QLHVHIYDTA KQQYQLPNGL IFDRPGDNPA DIQNGSTADQ 150
    SDLVFHHTAE NGTQSGNGGW AFWIARKSSG DVIFDTRASN IPTYNDGLSS 200
    VSSNTKRNTT AMPAHEMVFE NQYLQISSAL PTGANIYGLG EYVTGSFRRN 250
    PDETLQPFFT LDAGTPVDSN MYGYHPIYTE ARRGSDGKLR THSVHLQNTA 300
    GMDVLLRRGV IQYRAIGGTL DFRFFSGDQP ASSSSSSSGN DKAVATVKNS 350
    PNTAIQQYVN FIGNPVIHPY WSYGFHLCRW GYNNVSETQA VIDAMRQNNI 400
    PLEVQWNDID YLQEFRDFTT DPQRFPQKEF AAMIAKLKDN HQHYIPIIDM 450
    AIPKAPTNDT DVYYPGTRGD ELDVFIKNRN GSQYIGEVWP GYTNFVDQQA 500
    ENAGKWWTEA IRNFSEIVDF SGIWLDMNEP SSFVIGNAAG PETNLSNTPA 550
    YTAATSVAGW PQGYNNLTWG TSGNITVNGS YTYQQGPVQN NDGSKQRRSL 600
    LLSRDEDVLV QRDINVNGGN GDKFGPEDPN YQYANSSQRY LSNPPYAIHN 650
    GIHISETPLN VNLDKKTVAM EAVGVDGQRA FYDVHNLDGT LEEQHFYNAL 700
    RDIRPQERPF LISRSTYPGA GKFTGHWLGD NYALWTILPG EEAYKAGAGM 750
    AQSIDGVLQF QIFGIHLIGA DICGFNRNSD EELCNRWMML GAFLPFMRNH 800
    NTIGAIAQEP FRWDSVANAS RIAINKRYEI LPSLYSHMAQ SAESGEPAVR 850
    ALWYEFDEVF EQTKDYAHQF LFGDDLLVSP VLEPNVTQIK ALFPNAGGKW 900
    RNVFSYEALD VEYNKNVTVD AALSTINVHL RPGKVLLTHS KPAYTVYETA 950
    QSPYGLIVNL NDQGEAKQTF YLDDGMTPAP TPNSTLTVSA GNNSVNGSIE 1000
    GEYKAQQNLT YVVVLDVKQK PTQVMMGGNK TEFSWDQQKT LLNVTGLNAD 1050
    LNGSGRFRGL RLELSLLCED 1070
    Length:1,070
    Mass (Da):118,631
    Last modified:December 1, 1992 - v1
    Checksum:iEE990FAA0770FA4B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56024 Genomic DNA. Translation: CAA39501.1.
    PIRiS19686.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56024 Genomic DNA. Translation: CAA39501.1 .
    PIRi S19686.

    3D structure databases

    ProteinModelPortali P29064.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH31. Glycoside Hydrolase Family 31.
    mycoCLAPi AGL31A_CANTS.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF01055. Glyco_hydro_31. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 2 hits.
    SSF74650. SSF74650. 1 hit.
    PROSITEi PS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
    PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure and processing of the Candida tsukubaensis alpha-glucosidase. Homology with the rabbit intestinal sucrase-isomaltase complex and human lysosomal alpha-glucosidase."
      Kinsella B.T., Hogan S., Larkin A., Cantwell B.A.
      Eur. J. Biochem. 202:657-664(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 36-49 AND 613-634.
      Strain: CBS 6389.

    Entry informationi

    Entry nameiAGLU_CANTS
    AccessioniPrimary (citable) accession number: P29064
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 58 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

    Direct protein sequencing

    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