Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 163 (08 May 2019)
Sequence version 2 (01 Feb 1995)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Glucoamylase, intracellular sporulation-specific

Gene

SGA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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 sitei198SubstrateBy 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 sitei261Proton acceptorPROSITE-ProRule annotation1
Active sitei264Proton 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

  • glucan 1,4-alpha-glucosidase activity Source: SGD

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, Sporulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:YIL099W-MONOMER
YEAST:YIL099W-MONOMER

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH15 Glycoside Hydrolase Family 15

<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, intracellular sporulation-specific (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:SGA1
Synonyms:SGA
Ordered Locus Names:YIL099W
<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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<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 identifieri559292 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<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
  • UP000002311 <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 IX

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YIL099W

Saccharomyces Genome Database

More...
SGDi
S000001361 SGA1

<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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1075248

<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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001861201 – 549Glucoamylase, intracellular sporulation-specificAdd BLAST549

Proteomic databases

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

More...
PaxDbi
P08019

PRoteomics IDEntifications database

More...
PRIDEi
P08019

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
34892, 27 interactors

Protein interaction database and analysis system

More...
IntActi
P08019, 1 interactor

Molecular INTeraction database

More...
MINTi
P08019

STRING: functional protein association networks

More...
STRINGi
4932.YIL099W

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P08019

<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
P08019

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

<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

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000182646

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P08019

KEGG Orthology (KO)

More...
KOi
K01178

Identification of Orthologs from Complete Genome Data

More...
OMAi
EGNPWFI

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.50.10.10, 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
IPR011613 GH15-like
IPR000165 Glucoamylase

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00736 GLHYDRLASE15

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48208 SSF48208, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
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.

P08019-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARQKMFYNK LLGMLSVGFG FAWALENITI YEFDFGKGIL DQSYGGVFSN
60 70 80 90 100
NGPSQVQLRD AVLMNGTVVY DSNGAWDSSA LEEWLQGQKK VSIEKIFENI
110 120 130 140 150
GPSAVYPSIS PGVVIASPSQ THPDYFYQWI RDSALTINSI VSHSAGPAIE
160 170 180 190 200
TLLQYLNVSF HLQRSNNTLG AGIGYTNDTV ALGDPKWNVD NTAFTEDWGR
210 220 230 240 250
PQNDGPALRS IAILKIIDYI KQSGTDLGAK YPFQSTADIF DDIVRWDLRF
260 270 280 290 300
IIDHWNSSGF DLWEEVNGMH FFTLLVQLSA VDKSLSYFNA SERSSPFVEE
310 320 330 340 350
LRQTRRDISK FLVDPANGFI NGKYNYIVGT PMIADTLRSG LDISTLLAAN
360 370 380 390 400
TVHDAPSASH LPFDINDPAV LNTLHHLMLH MRSIYPINDS SKNATGIALG
410 420 430 440 450
RYPEDVYDGY GFGEGNPWVL ATCTASTTLY QLIYRHISEQ HDLVVPMNND
460 470 480 490 500
CSNAFWSELV FSNLTTLGND EGYLILEFNT PAFNQTIQKI FQLADSFLVK
510 520 530 540
LKAHVGTDGE LSEQFNKYTG FMQGAQHLTW SYTSFWDAYQ IRQEVLQSL
Length:549
Mass (Da):61,463
Last modified:February 1, 1995 - v2
<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:i6351E84F2CF4AB77
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti184D → H in CAA32071 (PubMed:3141213).Curated1
Sequence conflicti504 – 549HVGTD…VLQSL → TWEQTGN in AAA35042 (PubMed:3106330).CuratedAdd BLAST46

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
Z38125 Genomic DNA Translation: CAA86282.1
M16166 Genomic DNA Translation: AAA35042.1
X13858 Genomic DNA Translation: CAA32071.1
BK006942 Genomic DNA Translation: DAA08454.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S48474

NCBI Reference Sequences

More...
RefSeqi
NP_012167.3, NM_001179447.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YIL099W_mRNA; YIL099W_mRNA; YIL099W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
854708

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YIL099W

<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
Z38125 Genomic DNA Translation: CAA86282.1
M16166 Genomic DNA Translation: AAA35042.1
X13858 Genomic DNA Translation: CAA32071.1
BK006942 Genomic DNA Translation: DAA08454.1
PIRiS48474
RefSeqiNP_012167.3, NM_001179447.3

3D structure databases

SMRiP08019
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34892, 27 interactors
IntActiP08019, 1 interactor
MINTiP08019
STRINGi4932.YIL099W

Chemistry databases

BindingDBiP08019
ChEMBLiCHEMBL1075248

Protein family/group databases

CAZyiGH15 Glycoside Hydrolase Family 15

Proteomic databases

PaxDbiP08019
PRIDEiP08019

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL099W_mRNA; YIL099W_mRNA; YIL099W
GeneIDi854708
KEGGisce:YIL099W

Organism-specific databases

EuPathDBiFungiDB:YIL099W
SGDiS000001361 SGA1

Phylogenomic databases

HOGENOMiHOG000182646
InParanoidiP08019
KOiK01178
OMAiEGNPWFI

Enzyme and pathway databases

BioCyciMetaCyc:YIL099W-MONOMER
YEAST:YIL099W-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P08019

Family and domain databases

Gene3Di1.50.10.10, 1 hit
InterProiView protein in InterPro
IPR008928 6-hairpin_glycosidase_sf
IPR012341 6hp_glycosidase-like_sf
IPR011613 GH15-like
IPR000165 Glucoamylase
PfamiView protein in Pfam
PF00723 Glyco_hydro_15, 1 hit
PRINTSiPR00736 GLHYDRLASE15
SUPFAMiSSF48208 SSF48208, 1 hit
PROSITEiView protein in PROSITE
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_YEAST
<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: P08019
Secondary accession number(s): D6VVI8, Q07070
<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, 1988
Last sequence update: February 1, 1995
Last modified: May 8, 2019
This is version 163 of the entry and version 2 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. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families
  4. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again