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Entry version 108 (08 May 2019)
Sequence version 1 (01 Aug 1991)
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Protein

Glucoamylase

Gene

glaA

Organism
Aspergillus shirousami
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

<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 (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose. EC:3.2.1.3

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei143SubstrateBy similarity1
<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 sitei199Proton acceptorPROSITE-ProRule annotation1
Active sitei202Proton donorPROSITE-ProRule annotation1

<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
Biological processCarbohydrate metabolism, Polysaccharide degradation

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
CBM20 Carbohydrate-Binding Module Family 20
GH15 Glycoside Hydrolase Family 15

mycoCLAP, a database of fungal genes encoding lignocellulose-active proteins

More...
mycoCLAPi
GLA15A_ASPSH

<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:
Glucoamylase (EC:3.2.1.3)
Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase
<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:glaA
Synonyms:gla
<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 shirousami
<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 identifieri5070 [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 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 – 18Sequence analysisAdd BLAST18
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000000146719 – 24By similarity6
<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_000000146825 – 639GlucoamylaseAdd BLAST615

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi194N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi205N-linked (GlcNAc...) asparagineSequence analysis1
<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 bondi233 ↔ 236By similarity
Disulfide bondi245 ↔ 472By similarity
Disulfide bondi285 ↔ 293By similarity
Glycosylationi418N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi464O-linked (Man) serineBy similarity1
Glycosylationi466O-linked (Man) serineBy similarity1
Glycosylationi467O-linked (Man) serineBy similarity1
Glycosylationi475O-linked (Man) threonineBy similarity1
Glycosylationi476O-linked (Man) serineBy similarity1
Glycosylationi482O-linked (Man) serineBy similarity1
Glycosylationi483O-linked (Man) serineBy similarity1
Glycosylationi485O-linked (Man) threonineBy similarity1
Glycosylationi487O-linked (Man) threonineBy similarity1
Glycosylationi488O-linked (Man) serineBy similarity1
Glycosylationi491O-linked (Man) serineBy similarity1
Glycosylationi495O-linked (Man) threonineBy similarity1
Glycosylationi498O-linked (Man) threonineBy similarity1
Glycosylationi499O-linked (Man) threonineBy similarity1
Glycosylationi500O-linked (Man) threonineBy similarity1
Glycosylationi501O-linked (Man) threonineBy similarity1
Glycosylationi503O-linked (Man) threonineBy similarity1
Glycosylationi505O-linked (Man) threonineBy similarity1
Glycosylationi507O-linked (Man) serineBy similarity1
Glycosylationi511O-linked (Man) threonineBy similarity1
Glycosylationi512O-linked (Man) serineBy similarity1
Glycosylationi513O-linked (Man) threonineBy similarity1
Glycosylationi514O-linked (Man) serineBy similarity1
Glycosylationi516O-linked (Man) threonineBy similarity1
Glycosylationi517O-linked (Man) threonineBy similarity1
Glycosylationi519O-linked (Man) threonineBy similarity1
Glycosylationi521O-linked (Man) serineBy similarity1
Glycosylationi523O-linked (Man) threonineBy similarity1
Glycosylationi524O-linked (Man) serineBy similarity1
Glycosylationi525O-linked (Man) threonineBy similarity1
Glycosylationi527O-linked (Man) threonineBy similarity1
Glycosylationi528O-linked (Man) serineBy similarity1
Glycosylationi529O-linked (Man) serineBy similarity1
Glycosylationi530O-linked (Man) threonineBy similarity1
Glycosylationi531O-linked (Man) serineBy similarity1
Glycosylationi533O-linked (Man) threonineBy similarity1
Glycosylationi534O-linked (Man) threonineBy similarity1

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

<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
P22832

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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>Domaini532 – 639CBM20PROSITE-ProRule annotationAdd BLAST108

<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 15 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05811 CBM20_glucoamylase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.50.10.10, 1 hit
2.60.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008928 6-hairpin_glycosidase_sf
IPR012341 6hp_glycosidase-like_sf
IPR013784 Carb-bd-like_fold
IPR034836 CBM20_glucoamylase
IPR002044 CBM_fam20
IPR011613 GH15-like
IPR000165 Glucoamylase
IPR008291 Glucoamylase_SBD
IPR013783 Ig-like_fold

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00686 CBM_20, 1 hit
PF00723 Glyco_hydro_15, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001031 Glu-a-glcsd_SBD, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00736 GLHYDRLASE15

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01065 CBM_2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48208 SSF48208, 1 hit
SSF49452 SSF49452, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51166 CBM20, 1 hit
PS00820 GLUCOAMYLASE, 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.

P22832-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSFRSLLALS GLVCSGLASV ISKRATLDSW LSNEATVART AILNNIGADG
60 70 80 90 100
AWVSGADSGI VVASPSTDNP DYFYTWTRDS GIVLKTLVDL FRNGDTDLLS
110 120 130 140 150
TIEHYISSQA IIQGVSNPSG DLSSGGLGEP KFNVDETAYA GSWGRPQRDG
160 170 180 190 200
PALRATAMIG FGQWLLDNGY TSAATEIVWP LVRNDLSYVA QYWNQTGYDL
210 220 230 240 250
WEEVNGSSFF TIAVQHRALV EGSAFATAVG SSCSWCDSQA PQILCYLQSF
260 270 280 290 300
WTGSYILANF DSSRSGKDTN TLLGSIHTFD PEAGCDDSTF QPCSPRALAN
310 320 330 340 350
HKEVVDSFRS IYTLNDGLSD SEAVAVGRYP EDSYYNGNPW FLCTLAAAEQ
360 370 380 390 400
LYDALYQWDK QGSLEITDVS LDFFKALYSG AATGTYSSSS STYSSIVSAV
410 420 430 440 450
KTFADGFVSI VETHAASNGS LSEQFDKSDG DELSARDLTW SYAALLTANN
460 470 480 490 500
RRNSVVPPSW GETSASSVPG TCAATSASGT YSSVTVTSWP SIVATGGTTT
510 520 530 540 550
TATTTGSGGV TSTSKTTTTA SKTSTTTSST SCTTPTAVAV TFDLTATTTY
560 570 580 590 600
GENIYLVGSI SQLGDWETSD GIALSADKYT SSNPPWYVTV TLPAGESFEY
610 620 630
KFIRVESDDS VEWESDPNRE YTVPQACGES TATVTDTWR
Length:639
Mass (Da):68,131
Last modified:August 1, 1991 - 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:iE93DAE55EED72326
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D10460 Genomic DNA Translation: BAA01254.1

<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
D10460 Genomic DNA Translation: BAA01254.1

3D structure databases

SMRiP22832
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM20 Carbohydrate-Binding Module Family 20
GH15 Glycoside Hydrolase Family 15
mycoCLAPiGLA15A_ASPSH

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd05811 CBM20_glucoamylase, 1 hit
Gene3Di1.50.10.10, 1 hit
2.60.40.10, 1 hit
InterProiView protein in InterPro
IPR008928 6-hairpin_glycosidase_sf
IPR012341 6hp_glycosidase-like_sf
IPR013784 Carb-bd-like_fold
IPR034836 CBM20_glucoamylase
IPR002044 CBM_fam20
IPR011613 GH15-like
IPR000165 Glucoamylase
IPR008291 Glucoamylase_SBD
IPR013783 Ig-like_fold
PfamiView protein in Pfam
PF00686 CBM_20, 1 hit
PF00723 Glyco_hydro_15, 1 hit
PIRSFiPIRSF001031 Glu-a-glcsd_SBD, 1 hit
PRINTSiPR00736 GLHYDRLASE15
SMARTiView protein in SMART
SM01065 CBM_2, 1 hit
SUPFAMiSSF48208 SSF48208, 1 hit
SSF49452 SSF49452, 1 hit
PROSITEiView protein in PROSITE
PS51166 CBM20, 1 hit
PS00820 GLUCOAMYLASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiAMYG_ASPSH
<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: P22832
<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: August 1, 1991
Last sequence update: August 1, 1991
Last modified: May 8, 2019
This is version 108 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

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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