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Protein

Probable alpha-galactosidase A

Gene

aglA

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides.By similarity

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
Active sitei154NucleophileBy similarity1
Active sitei212Proton donorBy similarity1

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB-KW
  • galactosidase activity Source: ASPGD
  • hydrolase activity, acting on glycosyl bonds Source: ASPGD
  • raffinose alpha-galactosidase activity Source: UniProtKB-EC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Lectin

Enzyme and pathway databases

BRENDAi3.2.1.49. 518.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GH27. Glycoside Hydrolase Family 27.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable alpha-galactosidase A (EC:3.2.1.22)
Alternative name(s):
Melibiase A
Gene namesi
Name:aglA
ORF Names:An06g00170
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006706 Componenti: Chromosome 8ER

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_500022003224 – 537Probable alpha-galactosidase AAdd BLAST514

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi46 ↔ 78PROSITE-ProRule annotation
Glycosylationi49N-linked (GlcNAc...)Sequence analysis1
Glycosylationi87N-linked (GlcNAc...)Sequence analysis1
Glycosylationi93N-linked (GlcNAc...)Sequence analysis1
Glycosylationi123N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi126 ↔ 156PROSITE-ProRule annotation
Glycosylationi203N-linked (GlcNAc...)Sequence analysis1
Glycosylationi355N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi430 ↔ 444PROSITE-ProRule annotation
Glycosylationi436N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi469 ↔ 482PROSITE-ProRule annotation
Glycosylationi491N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliA2QL72.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini413 – 537Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST125

Sequence similaritiesi

Belongs to the glycosyl hydrolase 27 family.Curated
Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000161224.
KOiK07407.
OrthoDBiEOG092C1MJ6.

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.
IPR017853. Glycoside_hydrolase_SF.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF16499. Melibiase_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
PRINTSiPR00740. GLHYDRLASE27.
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00512. ALPHA_GALACTOSIDASE. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A2QL72-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQGTKSILL AATLAAIPWQ VYGSIEQSSL LPIPPMGFNN WARFMCDLNE
60 70 80 90 100
TLFTETADAM AANGLRDAGY NRINLDDCWM AYQRSDNGSL QWNTTKFPHG
110 120 130 140 150
LPWLAQYVKA KGFHFGIYED SGNMTCGGYP GSYNHEEQDA NTFALWGIDY
160 170 180 190 200
LKLDGCNVYA TQGRTLEEEY KQRYGHWHQV LSKMQHPLIF SESAPAYFAG
210 220 230 240 250
TDNNTDWYTV MDWVPIYGEL ARHSTDILVY SGAGSAWDSI MNNYNYNTLL
260 270 280 290 300
ARYQRPGYFN DPDFLIPDHP GLTADEKRSH FALWASFSAP LIISAYIPAL
310 320 330 340 350
SKDEIAFLTN EALIAVNQDP LAQQATFASR DNTLDILTRN LANGDRLLTV
360 370 380 390 400
LNKGNTTVTR DIPVQWLGLT ETDCTYTAED LWDGKTQKIS DHIKIELASH
410 420 430 440 450
ATAVFRLGLP QGCSSVVPTG LVFNTASGNC LTAASNSSVA FQSCNGETSQ
460 470 480 490 500
IWQVTLSGVI RPVSQTTQCL AADGNSVKLQ ACDSTDSDGQ NWTYAVTGNL
510 520 530
KNAKTDGCLT EGSVQMKSCL YERDGQVFGL PSGVQLS
Length:537
Mass (Da):59,213
Last modified:March 6, 2007 - v1
Checksum:iF093FD8196C7F839
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270108 Genomic DNA. Translation: CAK44933.1.
RefSeqiXP_001390845.1. XM_001390808.1.

Genome annotation databases

EnsemblFungiiCAK44933; CAK44933; An06g00170.
GeneIDi4981013.
KEGGiang:ANI_1_6054.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270108 Genomic DNA. Translation: CAK44933.1.
RefSeqiXP_001390845.1. XM_001390808.1.

3D structure databases

ProteinModelPortaliA2QL72.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GH27. Glycoside Hydrolase Family 27.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAK44933; CAK44933; An06g00170.
GeneIDi4981013.
KEGGiang:ANI_1_6054.

Phylogenomic databases

HOGENOMiHOG000161224.
KOiK07407.
OrthoDBiEOG092C1MJ6.

Enzyme and pathway databases

BRENDAi3.2.1.49. 518.

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.
IPR017853. Glycoside_hydrolase_SF.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF16499. Melibiase_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
PRINTSiPR00740. GLHYDRLASE27.
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00512. ALPHA_GALACTOSIDASE. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAGALA_ASPNC
AccessioniPrimary (citable) accession number: A2QL72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 6, 2007
Last modified: November 30, 2016
This is version 58 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

Complete proteome, Reference proteome

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.