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Protein

Alpha-galactosidase 1

Gene

MEL1

Organism
Saccharomyces cerevisiae (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei72 – 721Substrate
Binding sitei73 – 731Substrate
Binding sitei147 – 1471Substrate
Active sitei149 – 1491Nucleophile1 Publication
Binding sitei205 – 2051Substrate
Active sitei209 – 2091Proton donor1 Publication
Binding sitei251 – 2511Substrate

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.22. 984.

Protein family/group databases

CAZyiGH27. Glycoside Hydrolase Family 27.
mycoCLAPiMEL27A_YEAST.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-galactosidase 1 (EC:3.2.1.22)
Alternative name(s):
Alpha-D-galactoside galactohydrolase 1
Melibiase 1
Gene namesi
Name:MEL1
OrganismiSaccharomyces cerevisiae (Baker's yeast)
Taxonomic identifieri4932 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Organism-specific databases

SGDiS000029662. MEL1.

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Chaini19 – 471453Alpha-galactosidase 1PRO_0000001013Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 741 Publication
Glycosylationi105 – 1051N-linked (GlcNAc...)1 Publication
Disulfide bondi121 ↔ 1511 Publication
Glycosylationi175 – 1751N-linked (GlcNAc...)1 Publication
Disulfide bondi221 ↔ 2371 Publication
Disulfide bondi223 ↔ 2301 Publication
Glycosylationi270 – 2701N-linked (GlcNAc...)1 Publication
Glycosylationi370 – 3701N-linked (GlcNAc...)1 Publication
Glycosylationi403 – 4031N-linked (GlcNAc...)1 Publication
Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence analysis
Glycosylationi422 – 4221N-linked (GlcNAc...)1 Publication
Glycosylationi435 – 4351N-linked (GlcNAc...)Sequence analysis
Glycosylationi454 – 4541N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Inductioni

Induced by galactose and melibiose and repressed by glucose.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

DIPiDIP-1369N.
IntActiP04824. 1 interaction.
MINTiMINT-409665.

Structurei

Secondary structure

1
471
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 253Combined sources
Beta strandi32 – 365Combined sources
Helixi37 – 404Combined sources
Helixi46 – 5813Combined sources
Helixi62 – 643Combined sources
Beta strandi68 – 703Combined sources
Beta strandi76 – 794Combined sources
Beta strandi85 – 873Combined sources
Turni89 – 913Combined sources
Helixi96 – 10510Combined sources
Beta strandi109 – 11911Combined sources
Beta strandi123 – 1253Combined sources
Helixi131 – 14010Combined sources
Beta strandi145 – 1495Combined sources
Helixi160 – 17718Combined sources
Beta strandi182 – 1854Combined sources
Turni188 – 1925Combined sources
Helixi193 – 1964Combined sources
Turni198 – 2003Combined sources
Beta strandi202 – 2054Combined sources
Helixi239 – 2468Combined sources
Helixi247 – 2526Combined sources
Beta strandi257 – 2604Combined sources
Helixi273 – 28513Combined sources
Beta strandi290 – 2923Combined sources
Helixi296 – 2983Combined sources
Helixi301 – 3077Combined sources
Helixi310 – 3167Combined sources
Beta strandi325 – 3317Combined sources
Beta strandi342 – 3498Combined sources
Beta strandi355 – 3617Combined sources
Beta strandi363 – 3653Combined sources
Beta strandi367 – 3715Combined sources
Helixi373 – 3764Combined sources
Turni377 – 3793Combined sources
Helixi385 – 3884Combined sources
Beta strandi391 – 3955Combined sources
Turni396 – 3994Combined sources
Helixi403 – 4108Combined sources
Turni417 – 4193Combined sources
Turni423 – 4253Combined sources
Helixi428 – 4336Combined sources
Helixi437 – 4404Combined sources
Beta strandi442 – 4476Combined sources
Beta strandi453 – 4575Combined sources
Beta strandi461 – 4699Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LRKX-ray1.95A1-471[»]
3LRLX-ray2.40A1-471[»]
3LRMX-ray2.70A/B/C/D1-471[»]
ProteinModelPortaliP04824.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04824.

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.
IPR000111. Glyco_hydro_27/36_CS.
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.
PROSITEiPS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P04824-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFAFYFLTAC ISLKGVFGVS PSYNGLGLTP QMGWDNWNTF ACDVSEQLLL
60 70 80 90 100
DTADRISDLG LKDMGYKYII LDDCWSSGRD SDGFLVADEQ KFPNGMGHVA
110 120 130 140 150
DHLHNNSFLF GMYSSAGEYT CAGYPGSLGR EEEDAQFFAN NRVDYLKYDN
160 170 180 190 200
CYNKGQFGTP EISYHRYKAM SDALNKTGRP IFYSLCNWGQ DLTFYWGSGI
210 220 230 240 250
ANSWRMSGDV TAEFTRPDSR CPCDGDEYDC KYAGFHCSIM NILNKAAPMG
260 270 280 290 300
QNAGVGGWND LDNLEVGVGN LTDDEEKAHF SMWAMVKSPL IIGANVNNLK
310 320 330 340 350
ASSYSIYSQA SVIAINQDSN GIPATRVWRY YVSDTDEYGQ GEIQMWSGPL
360 370 380 390 400
DNGDQVVALL NGGSVSRPMN TTLEEIFFDS NLGSKKLTST WDIYDLWANR
410 420 430 440 450
VDNSTASAIL GRNKTATGIL YNATEQSYKD GLSKNDTRLF GQKIGSLSPN
460 470
AILNTTVPAH GIAFYRLRPS S
Length:471
Mass (Da):52,102
Last modified:August 13, 1987 - v1
Checksum:i7A2E265A6BA09DBD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03102 Genomic DNA. Translation: CAA26888.1.
M10604 Genomic DNA. Translation: AAA34770.1.
PIRiA00897. GBBYAG.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03102 Genomic DNA. Translation: CAA26888.1.
M10604 Genomic DNA. Translation: AAA34770.1.
PIRiA00897. GBBYAG.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LRKX-ray1.95A1-471[»]
3LRLX-ray2.40A1-471[»]
3LRMX-ray2.70A/B/C/D1-471[»]
ProteinModelPortaliP04824.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-1369N.
IntActiP04824. 1 interaction.
MINTiMINT-409665.

Protein family/group databases

CAZyiGH27. Glycoside Hydrolase Family 27.
mycoCLAPiMEL27A_YEAST.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

SGDiS000029662. MEL1.

Enzyme and pathway databases

BRENDAi3.2.1.22. 984.

Miscellaneous databases

EvolutionaryTraceiP04824.

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.
IPR000111. Glyco_hydro_27/36_CS.
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.
PROSITEiPS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMEL1_YEASX
AccessioniPrimary (citable) accession number: P04824
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: September 7, 2016
This is version 101 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

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.