Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Binding sitei72Substrate1
Binding sitei73Substrate1
Binding sitei147Substrate1
Active sitei149Nucleophile1 Publication1
Binding sitei205Substrate1
Active sitei209Proton donor1 Publication1
Binding sitei251Substrate1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Add BLAST18
ChainiPRO_000000101319 – 471Alpha-galactosidase 1Add BLAST453

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi42 ↔ 741 Publication
Glycosylationi105N-linked (GlcNAc...)1 Publication1
Disulfide bondi121 ↔ 1511 Publication
Glycosylationi175N-linked (GlcNAc...)1 Publication1
Disulfide bondi221 ↔ 2371 Publication
Disulfide bondi223 ↔ 2301 Publication
Glycosylationi270N-linked (GlcNAc...)1 Publication1
Glycosylationi370N-linked (GlcNAc...)1 Publication1
Glycosylationi403N-linked (GlcNAc...)1 Publication1
Glycosylationi413N-linked (GlcNAc...)Sequence analysis1
Glycosylationi422N-linked (GlcNAc...)1 Publication1
Glycosylationi435N-linked (GlcNAc...)Sequence analysis1
Glycosylationi454N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP04824.

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 interactor.
MINTiMINT-409665.

Structurei

Secondary structure

1471
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 25Combined sources3
Beta strandi32 – 36Combined sources5
Helixi37 – 40Combined sources4
Helixi46 – 58Combined sources13
Helixi62 – 64Combined sources3
Beta strandi68 – 70Combined sources3
Beta strandi76 – 79Combined sources4
Beta strandi85 – 87Combined sources3
Turni89 – 91Combined sources3
Helixi96 – 105Combined sources10
Beta strandi109 – 119Combined sources11
Beta strandi123 – 125Combined sources3
Helixi131 – 140Combined sources10
Beta strandi145 – 149Combined sources5
Helixi160 – 177Combined sources18
Beta strandi182 – 185Combined sources4
Turni188 – 192Combined sources5
Helixi193 – 196Combined sources4
Turni198 – 200Combined sources3
Beta strandi202 – 205Combined sources4
Helixi239 – 246Combined sources8
Helixi247 – 252Combined sources6
Beta strandi257 – 260Combined sources4
Helixi273 – 285Combined sources13
Beta strandi290 – 292Combined sources3
Helixi296 – 298Combined sources3
Helixi301 – 307Combined sources7
Helixi310 – 316Combined sources7
Beta strandi325 – 331Combined sources7
Beta strandi342 – 349Combined sources8
Beta strandi355 – 361Combined sources7
Beta strandi363 – 365Combined sources3
Beta strandi367 – 371Combined sources5
Helixi373 – 376Combined sources4
Turni377 – 379Combined sources3
Helixi385 – 388Combined sources4
Beta strandi391 – 395Combined sources5
Turni396 – 399Combined sources4
Helixi403 – 410Combined sources8
Turni417 – 419Combined sources3
Turni423 – 425Combined sources3
Helixi428 – 433Combined sources6
Helixi437 – 440Combined sources4
Beta strandi442 – 447Combined sources6
Beta strandi453 – 457Combined sources5
Beta strandi461 – 469Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LRKX-ray1.95A1-471[»]
3LRLX-ray2.40A1-471[»]
3LRMX-ray2.70A/B/C/D1-471[»]
ProteinModelPortaliP04824.
SMRiP04824.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LRKX-ray1.95A1-471[»]
3LRLX-ray2.40A1-471[»]
3LRMX-ray2.70A/B/C/D1-471[»]
ProteinModelPortaliP04824.
SMRiP04824.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

CAZyiGH27. Glycoside Hydrolase Family 27.
mycoCLAPiMEL27A_YEAST.

Proteomic databases

PRIDEiP04824.

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: November 2, 2016
This is version 103 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.