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Protein

Alpha-glucosidase

Gene
N/A
Organism
Candida tsukubaensis (Yeast) (Pseudozyma tsukubaensis)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
Active sitei526NucleophilePROSITE-ProRule annotation1
Active sitei529By similarity1
Active sitei730Proton donorBy similarity1

GO - Molecular functioni

Complete GO annotation...

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 lineageiEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaePseudozyma

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 351 PublicationAdd BLAST35
ChainiPRO_000001857836 – 612Alpha-glucosidase subunit 1Add BLAST577
ChainiPRO_0000018579613 – 1070Alpha-glucosidase subunit 2Add BLAST458

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi48N-linked (GlcNAc...)Sequence analysis1
Glycosylationi99N-linked (GlcNAc...)Sequence analysis1
Glycosylationi144N-linked (GlcNAc...)Sequence analysis1
Glycosylationi161N-linked (GlcNAc...)Sequence analysis1
Glycosylationi208N-linked (GlcNAc...)Sequence analysis1
Glycosylationi384N-linked (GlcNAc...)Sequence analysis1
Glycosylationi458N-linked (GlcNAc...)Sequence analysis1
Glycosylationi480N-linked (GlcNAc...)Sequence analysis1
Glycosylationi513N-linked (GlcNAc...)Sequence analysis1
Glycosylationi544N-linked (GlcNAc...)Sequence analysis1
Glycosylationi566N-linked (GlcNAc...)Sequence analysis1
Glycosylationi574N-linked (GlcNAc...)Sequence analysis1
Glycosylationi578N-linked (GlcNAc...)Sequence analysis1
Glycosylationi635N-linked (GlcNAc...)Sequence analysis1
Glycosylationi818N-linked (GlcNAc...)Sequence analysis1
Glycosylationi885N-linked (GlcNAc...)Sequence analysis1
Glycosylationi916N-linked (GlcNAc...)Sequence analysis1
Glycosylationi983N-linked (GlcNAc...)Sequence analysis1
Glycosylationi992N-linked (GlcNAc...)Sequence analysis1
Glycosylationi996N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1008N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1029N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1043N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1052N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein, Zymogen

Proteomic databases

PRIDEiP29064.

Structurei

3D structure databases

ProteinModelPortaliP29064.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi332 – 338Poly-Ser7

Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR031727. Gal_mutarotase_N.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR030458. Glyco_hydro_31_AS.
IPR030459. Glyco_hydro_31_CS.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01055. Glyco_hydro_31. 1 hit.
PF16863. NtCtMGAM_N. 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

« Hide

        10         20         30         40         50
MRSIKAASLT PLLAALFTTL SSTLALPSSV WEHQLETNVL ALRDTNNNGS
60 70 80 90 100
SSTISPSFDV TKCPGYKLVG QPQQSQHGFT AQLSLAGDAC NAYGVDIANL
110 120 130 140 150
TLSVVYEKQH QLHVHIYDTA KQQYQLPNGL IFDRPGDNPA DIQNGSTADQ
160 170 180 190 200
SDLVFHHTAE NGTQSGNGGW AFWIARKSSG DVIFDTRASN IPTYNDGLSS
210 220 230 240 250
VSSNTKRNTT AMPAHEMVFE NQYLQISSAL PTGANIYGLG EYVTGSFRRN
260 270 280 290 300
PDETLQPFFT LDAGTPVDSN MYGYHPIYTE ARRGSDGKLR THSVHLQNTA
310 320 330 340 350
GMDVLLRRGV IQYRAIGGTL DFRFFSGDQP ASSSSSSSGN DKAVATVKNS
360 370 380 390 400
PNTAIQQYVN FIGNPVIHPY WSYGFHLCRW GYNNVSETQA VIDAMRQNNI
410 420 430 440 450
PLEVQWNDID YLQEFRDFTT DPQRFPQKEF AAMIAKLKDN HQHYIPIIDM
460 470 480 490 500
AIPKAPTNDT DVYYPGTRGD ELDVFIKNRN GSQYIGEVWP GYTNFVDQQA
510 520 530 540 550
ENAGKWWTEA IRNFSEIVDF SGIWLDMNEP SSFVIGNAAG PETNLSNTPA
560 570 580 590 600
YTAATSVAGW PQGYNNLTWG TSGNITVNGS YTYQQGPVQN NDGSKQRRSL
610 620 630 640 650
LLSRDEDVLV QRDINVNGGN GDKFGPEDPN YQYANSSQRY LSNPPYAIHN
660 670 680 690 700
GIHISETPLN VNLDKKTVAM EAVGVDGQRA FYDVHNLDGT LEEQHFYNAL
710 720 730 740 750
RDIRPQERPF LISRSTYPGA GKFTGHWLGD NYALWTILPG EEAYKAGAGM
760 770 780 790 800
AQSIDGVLQF QIFGIHLIGA DICGFNRNSD EELCNRWMML GAFLPFMRNH
810 820 830 840 850
NTIGAIAQEP FRWDSVANAS RIAINKRYEI LPSLYSHMAQ SAESGEPAVR
860 870 880 890 900
ALWYEFDEVF EQTKDYAHQF LFGDDLLVSP VLEPNVTQIK ALFPNAGGKW
910 920 930 940 950
RNVFSYEALD VEYNKNVTVD AALSTINVHL RPGKVLLTHS KPAYTVYETA
960 970 980 990 1000
QSPYGLIVNL NDQGEAKQTF YLDDGMTPAP TPNSTLTVSA GNNSVNGSIE
1010 1020 1030 1040 1050
GEYKAQQNLT YVVVLDVKQK PTQVMMGGNK TEFSWDQQKT LLNVTGLNAD
1060 1070
LNGSGRFRGL RLELSLLCED
Length:1,070
Mass (Da):118,631
Last modified:December 1, 1992 - v1
Checksum:iEE990FAA0770FA4B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56024 Genomic DNA. Translation: CAA39501.1.
PIRiS19686.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56024 Genomic DNA. Translation: CAA39501.1.
PIRiS19686.

3D structure databases

ProteinModelPortaliP29064.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.
mycoCLAPiAGL31A_CANTS.

Proteomic databases

PRIDEiP29064.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR031727. Gal_mutarotase_N.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR030458. Glyco_hydro_31_AS.
IPR030459. Glyco_hydro_31_CS.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01055. Glyco_hydro_31. 1 hit.
PF16863. NtCtMGAM_N. 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]
ProtoNetiSearch...

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 5, 2016
This is version 64 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.