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Entry version 73 (08 May 2019)
Sequence version 1 (06 Mar 2007)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Protein inferred from homologyi <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. EC:3.2.1.22

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei154NucleophileBy similarity1
Active sitei212Proton donorBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosidase, Hydrolase
LigandLectin

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.49 518

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
CBM13 Carbohydrate-Binding Module Family 13
GH27 Glycoside Hydrolase Family 27

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Probable alpha-galactosidase A (EC:3.2.1.22)
Alternative name(s):
Melibiase A
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:aglA
ORF Names:An06g00170
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri425011 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000006706 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8ER

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 23Sequence analysisAdd BLAST23
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_500022003224 – 537Probable alpha-galactosidase AAdd BLAST514

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi46 ↔ 78PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi49N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi87N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi93N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi123N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi126 ↔ 156PROSITE-ProRule annotation
Glycosylationi203N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi355N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi430 ↔ 444PROSITE-ProRule annotation
Glycosylationi436N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi469 ↔ 482PROSITE-ProRule annotation
Glycosylationi491N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
A2QL72

PRoteomics IDEntifications database

More...
PRIDEi
A2QL72

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
A2QL72

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini413 – 537Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST125

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyl hydrolase 27 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000161224

KEGG Orthology (KO)

More...
KOi
K07407

Family and domain databases

Conserved Domains Database

More...
CDDi
cd14792 GH27, 1 hit
cd00161 RICIN, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.1180, 1 hit
3.20.20.70, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013785 Aldolase_TIM
IPR002241 Glyco_hydro_27
IPR000111 Glyco_hydro_27/36_CS
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR041233 Melibiase_C
IPR035992 Ricin_B-like_lectins
IPR000772 Ricin_B_lectin

The PANTHER Classification System

More...
PANTHERi
PTHR11452 PTHR11452, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16499 Melibiase_2, 1 hit
PF17801 Melibiase_C, 1 hit
PF00652 Ricin_B_lectin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00740 GLHYDRLASE27

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00458 RICIN, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50370 SSF50370, 1 hit
SSF51445 SSF51445, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00512 ALPHA_GALACTOSIDASE, 1 hit
PS50231 RICIN_B_LECTIN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF093FD8196C7F839
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AM270108 Genomic DNA Translation: CAK44933.1

NCBI Reference Sequences

More...
RefSeqi
XP_001390845.1, XM_001390808.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
CAK44933; CAK44933; An06g00170

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4981013

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ang:ANI_1_6054

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

SMRiA2QL72
ModBaseiSearch...

Protein family/group databases

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

Proteomic databases

PaxDbiA2QL72
PRIDEiA2QL72

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAK44933; CAK44933; An06g00170
GeneIDi4981013
KEGGiang:ANI_1_6054

Phylogenomic databases

HOGENOMiHOG000161224
KOiK07407

Enzyme and pathway databases

BRENDAi3.2.1.49 518

Family and domain databases

CDDicd14792 GH27, 1 hit
cd00161 RICIN, 1 hit
Gene3Di2.60.40.1180, 1 hit
3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR002241 Glyco_hydro_27
IPR000111 Glyco_hydro_27/36_CS
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR041233 Melibiase_C
IPR035992 Ricin_B-like_lectins
IPR000772 Ricin_B_lectin
PANTHERiPTHR11452 PTHR11452, 1 hit
PfamiView protein in Pfam
PF16499 Melibiase_2, 1 hit
PF17801 Melibiase_C, 1 hit
PF00652 Ricin_B_lectin, 1 hit
PRINTSiPR00740 GLHYDRLASE27
SMARTiView protein in SMART
SM00458 RICIN, 1 hit
SUPFAMiSSF50370 SSF50370, 1 hit
SSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS00512 ALPHA_GALACTOSIDASE, 1 hit
PS50231 RICIN_B_LECTIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAGALA_ASPNC
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: A2QL72
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 6, 2007
Last modified: May 8, 2019
This is version 73 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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