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P29064

- AGLU_CANTS

UniProt

P29064 - AGLU_CANTS

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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

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. alpha-1,4-glucosidase activity Source: UniProtKB-EC
  2. carbohydrate binding Source: InterPro
  3. maltose alpha-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
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 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

« 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 .
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 29, 2014
This is version 59 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