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Protein

Alpha-galactosidase

Gene

MEL

Organism
Saccharomyces pastorianus (strain ATCC 76529 / Carlsberg bottom yeast no.1 / CBS 1513 / CLIB 176 / NBRC 1167 / NCYC 396 / NRRL Y-12693) (Saaz-type lager yeast) (Saccharomyces carlsbergensis)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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)DescriptionActionsGraphical viewLength
Binding sitei72SubstrateBy similarity1
Binding sitei73SubstrateBy similarity1
Binding sitei147SubstrateBy similarity1
Active sitei149NucleophileBy similarity1
Binding sitei205SubstrateBy similarity1
Active sitei209Proton donorBy similarity1
Binding sitei251SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH27. Glycoside Hydrolase Family 27.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-galactosidase (EC:3.2.1.22)
Alternative name(s):
Alpha-D-galactoside galactohydrolase
MELx
Melibiase
Gene namesi
Name:MEL
OrganismiSaccharomyces pastorianus (strain ATCC 76529 / Carlsberg bottom yeast no.1 / CBS 1513 / CLIB 176 / NBRC 1167 / NCYC 396 / NRRL Y-12693) (Saaz-type lager yeast) (Saccharomyces carlsbergensis)
Taxonomic identifieri1073566 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18By similarityAdd BLAST18
ChainiPRO_000000100919 – 471Alpha-galactosidaseAdd BLAST453

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi42 ↔ 74By similarity
Glycosylationi82N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi121 ↔ 151By similarity
Glycosylationi175N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi221 ↔ 237By similarity
Disulfide bondi223 ↔ 230By similarity
Glycosylationi270N-linked (GlcNAc...)Sequence analysis1
Glycosylationi403N-linked (GlcNAc...)Sequence analysis1
Glycosylationi412N-linked (GlcNAc...)Sequence analysis1
Glycosylationi417N-linked (GlcNAc...)Sequence analysis1
Glycosylationi422N-linked (GlcNAc...)Sequence analysis1
Glycosylationi435N-linked (GlcNAc...)Sequence analysis1
Glycosylationi454N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ03647.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 27 family.Curated

Keywords - Domaini

Signal

Family and domain databases

CDDicd14792. GH27. 1 hit.
Gene3Di2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002241. Glyco_hydro_27.
IPR013780. Glyco_hydro_b.
IPR006215. Glyco_hydro_melibiase.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF16499. Melibiase_2. 1 hit.
[Graphical view]
PRINTSiPR00740. GLHYDRLASE27.
PR00748. MELIBIASE.
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q03647-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLLYLFTSF AAVSGVLGSS PSYNGLGLTP QMGWDNWNTF ACDVSEQLLL
60 70 80 90 100
DTADRISEIG LKDLGYTYVI LDDCWSSGRT ANGTLVADKE KFPNGMSHVA
110 120 130 140 150
DHLHNNNFLF GMYSSAGEYT CAGYPGSLGH EEEDAEFFAS NGVDYLKYDN
160 170 180 190 200
CYNKGQFGAP ETSYKRYKAM SDALNKTGRP IFYSLCNWGQ DLTHYWGSDI
210 220 230 240 250
ANSWRMSGDI YPQFTRPDSR CPCDGDQFDC AYAGFHCSIM NILNKAAPMG
260 270 280 290 300
QNAGIGGWND LDNLEVGVGN LTDDEEKAHF SMWAMVKSPL VIGADVNHLK
310 320 330 340 350
ASSYSIYSQA SVIAINQDPK GVPATRVWRH QVPQTDKYGQ GEIQFWSGPL
360 370 380 390 400
DNGDQVIALL NGGIKPRPMN TNLEEIFFDS YLGFEQLSSN WDIYDLWANR
410 420 430 440 450
VDNATSANIL NNNSVGNATI YNATALSYKD GMAKNDTRLF GTKIGSISPD
460 470
GLLNTTVPAH GIAFYRLRRS T
Length:471
Mass (Da):52,000
Last modified:November 1, 1996 - v1
Checksum:iE49E27EC278C4A23
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58484 Genomic DNA. Translation: AAA34769.1.
PIRiJQ1021.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58484 Genomic DNA. Translation: AAA34769.1.
PIRiJQ1021.

3D structure databases

ProteinModelPortaliQ03647.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH27. Glycoside Hydrolase Family 27.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd14792. GH27. 1 hit.
Gene3Di2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002241. Glyco_hydro_27.
IPR013780. Glyco_hydro_b.
IPR006215. Glyco_hydro_melibiase.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF16499. Melibiase_2. 1 hit.
[Graphical view]
PRINTSiPR00740. GLHYDRLASE27.
PR00748. MELIBIASE.
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMEL_SACCA
AccessioniPrimary (citable) accession number: Q03647
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.