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P29064 (AGLU_CANTS) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-glucosidase

EC=3.2.1.20
Alternative name(s):
Maltase

Cleaved into the following 2 chains:

  1. Alpha-glucosidase subunit 1
  2. Alpha-glucosidase subunit 2
OrganismCandida tsukubaensis (Yeast) (Pseudozyma tsukubaensis)
Taxonomic identifier5483 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaemitosporic UstilaginaceaePseudozyma

Protein attributes

Sequence length1070 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 31 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

maltose alpha-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Ref.1
Chain36 – 612577Alpha-glucosidase subunit 1
PRO_0000018578
Chain613 – 1070458Alpha-glucosidase subunit 2
PRO_0000018579

Regions

Compositional bias332 – 3387Poly-Ser

Sites

Active site5261Nucleophile By similarity
Active site5291 By similarity
Active site7301Proton donor By similarity

Amino acid modifications

Glycosylation481N-linked (GlcNAc...) Potential
Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation1441N-linked (GlcNAc...) Potential
Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation2081N-linked (GlcNAc...) Potential
Glycosylation3841N-linked (GlcNAc...) Potential
Glycosylation4581N-linked (GlcNAc...) Potential
Glycosylation4801N-linked (GlcNAc...) Potential
Glycosylation5131N-linked (GlcNAc...) Potential
Glycosylation5441N-linked (GlcNAc...) Potential
Glycosylation5661N-linked (GlcNAc...) Potential
Glycosylation5741N-linked (GlcNAc...) Potential
Glycosylation5781N-linked (GlcNAc...) Potential
Glycosylation6351N-linked (GlcNAc...) Potential
Glycosylation8181N-linked (GlcNAc...) Potential
Glycosylation8851N-linked (GlcNAc...) Potential
Glycosylation9161N-linked (GlcNAc...) Potential
Glycosylation9831N-linked (GlcNAc...) Potential
Glycosylation9921N-linked (GlcNAc...) Potential
Glycosylation9961N-linked (GlcNAc...) Potential
Glycosylation10081N-linked (GlcNAc...) Potential
Glycosylation10291N-linked (GlcNAc...) Potential
Glycosylation10431N-linked (GlcNAc...) Potential
Glycosylation10521N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P29064 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: EE990FAA0770FA4B

FASTA1,070118,631
        10         20         30         40         50         60 
MRSIKAASLT PLLAALFTTL SSTLALPSSV WEHQLETNVL ALRDTNNNGS SSTISPSFDV 

        70         80         90        100        110        120 
TKCPGYKLVG QPQQSQHGFT AQLSLAGDAC NAYGVDIANL TLSVVYEKQH QLHVHIYDTA 

       130        140        150        160        170        180 
KQQYQLPNGL IFDRPGDNPA DIQNGSTADQ SDLVFHHTAE NGTQSGNGGW AFWIARKSSG 

       190        200        210        220        230        240 
DVIFDTRASN IPTYNDGLSS VSSNTKRNTT AMPAHEMVFE NQYLQISSAL PTGANIYGLG 

       250        260        270        280        290        300 
EYVTGSFRRN PDETLQPFFT LDAGTPVDSN MYGYHPIYTE ARRGSDGKLR THSVHLQNTA 

       310        320        330        340        350        360 
GMDVLLRRGV IQYRAIGGTL DFRFFSGDQP ASSSSSSSGN DKAVATVKNS PNTAIQQYVN 

       370        380        390        400        410        420 
FIGNPVIHPY WSYGFHLCRW GYNNVSETQA VIDAMRQNNI PLEVQWNDID YLQEFRDFTT 

       430        440        450        460        470        480 
DPQRFPQKEF AAMIAKLKDN HQHYIPIIDM AIPKAPTNDT DVYYPGTRGD ELDVFIKNRN 

       490        500        510        520        530        540 
GSQYIGEVWP GYTNFVDQQA ENAGKWWTEA IRNFSEIVDF SGIWLDMNEP SSFVIGNAAG 

       550        560        570        580        590        600 
PETNLSNTPA YTAATSVAGW PQGYNNLTWG TSGNITVNGS YTYQQGPVQN NDGSKQRRSL 

       610        620        630        640        650        660 
LLSRDEDVLV QRDINVNGGN GDKFGPEDPN YQYANSSQRY LSNPPYAIHN GIHISETPLN 

       670        680        690        700        710        720 
VNLDKKTVAM EAVGVDGQRA FYDVHNLDGT LEEQHFYNAL RDIRPQERPF LISRSTYPGA 

       730        740        750        760        770        780 
GKFTGHWLGD NYALWTILPG EEAYKAGAGM AQSIDGVLQF QIFGIHLIGA DICGFNRNSD 

       790        800        810        820        830        840 
EELCNRWMML GAFLPFMRNH NTIGAIAQEP FRWDSVANAS RIAINKRYEI LPSLYSHMAQ 

       850        860        870        880        890        900 
SAESGEPAVR ALWYEFDEVF EQTKDYAHQF LFGDDLLVSP VLEPNVTQIK ALFPNAGGKW 

       910        920        930        940        950        960 
RNVFSYEALD VEYNKNVTVD AALSTINVHL RPGKVLLTHS KPAYTVYETA QSPYGLIVNL 

       970        980        990       1000       1010       1020 
NDQGEAKQTF YLDDGMTPAP TPNSTLTVSA GNNSVNGSIE GEYKAQQNLT YVVVLDVKQK 

      1030       1040       1050       1060       1070 
PTQVMMGGNK TEFSWDQQKT LLNVTGLNAD LNGSGRFRGL RLELSLLCED 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56024 Genomic DNA. Translation: CAA39501.1.
PIRS19686.

3D structure databases

ProteinModelPortalP29064.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH31. Glycoside Hydrolase Family 31.
mycoCLAPAGL31A_CANTS.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 1 hit.
PROSITEPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAGLU_CANTS
AccessionPrimary (citable) accession number: P29064
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: October 16, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries