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Entry version 71 (17 Jun 2020)
Sequence version 1 (01 Aug 1991)
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Protein

Glucoamylase 1

Gene

GAM1

Organism
Schwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis)
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>
-Experimental evidence at protein leveli <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

This glucoamylase has a specificity toward both alpha-1,4 and alpha-1,6 linkages.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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.PROSITE-ProRule annotation EC:3.2.1.3

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei470By similarity1
Active sitei473By similarity1
Active sitei638Proton 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
Biological processCarbohydrate metabolism, Polysaccharide degradation

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH31, Glycoside Hydrolase Family 31

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

More...
CLAEi
GLA31A_DEBOC

<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%5Fand%5Ftaxonomy%5Fsection">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 1 (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%5Fand%5Ftaxonomy%5Fsection">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:GAM1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiSchwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri27300 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeSchwanniomyces

<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 – 22Sequence analysisAdd BLAST22
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001858623 – 958Glucoamylase 1Add BLAST936

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi61N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi78N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi107N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi197N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi403N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi416N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi513N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi580N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi602N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi813N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi907N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

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
P22861

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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi26 – 41Ser-richAdd BLAST16
Compositional biasi530 – 542Ser/Thr-richAdd BLAST13

<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 31 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.1180, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR031727, Gal_mutarotase_N
IPR011013, Gal_mutarotase_sf_dom
IPR000322, Glyco_hydro_31
IPR030458, Glyco_hydro_31_AS
IPR030459, Glyco_hydro_31_CS
IPR013780, Glyco_hydro_b
IPR017853, Glycoside_hydrolase_SF

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01055, Glyco_hydro_31, 1 hit
PF16863, NtCtMGAM_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51445, SSF51445, 1 hit
SSF74650, SSF74650, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00129, GLYCOSYL_HYDROL_F31_1, 1 hit
PS00707, GLYCOSYL_HYDROL_F31_2, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P22861-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIFLKLIKSI VIGLGLVSAI QAAPASSIGS SASASSSSES SQATIPNDVT
60 70 80 90 100
LGVKQIPNIF NDSAVDANAA AKGYDLVNVT NTPRGLTGIL KLKEATNIYG
110 120 130 140 150
YDFDYLNLTV EYQADTRLNV HIEPTDLSDV FVLPEHLVVK PLVEGDAQSY
160 170 180 190 200
NFDNSDLVFE YSNTDFSFEV IRSSTKEVLF STKGNPLVFS NQFIQFNSSL
210 220 230 240 250
PKNHVITGLG ESIHGLVNEP GSVKTLFAND VGDPIDGNIY GVHPVYLDQR
260 270 280 290 300
YDTETTHAVY WRTSAIQEVL IGEESITWRA LSGVIDLYFF SGPTPKDAIQ
310 320 330 340 350
QYVKEIGLPA FQPYWSLGYH QCRWGYDTIE KLSEVVENFK KFNIPLETIW
360 370 380 390 400
SDIDYMDSYK DFTYDPHRFP LDEYRKFLDE LHKNNQHYVP ILDAAIYVPN
410 420 430 440 450
PNNATDNEYQ PFHYGNETDV FLKNPDGSLY IGAVWQVTLF SRFLSRKHSD
460 470 480 490 500
MDKVIKDWYE LTPFDGIWAD MNEVSSFCVG SCGTGKYFEN PAYPPFTVGS
510 520 530 540 550
KATSYPVGFD VSNASEWKSI QSSISATAKT SSTSSVSSSS STIDYMNTLA
560 570 580 590 600
PGKGNINYPP YAIYNMQGDS DLATHAVSPN ATHADGTVEY DIHNLYGYLQ
610 620 630 640 650
ENATYHALLE VFPNKRPFMI SRSTFPRAGK WTGHWGGDNT ADWAYAYFSI
660 670 680 690 700
PQAFSMGIAG LPFFGADVCG FNGNSDSELC SRWMQLGSFF PFYRNHNYLG
710 720 730 740 750
AIDQEPYVWE SVAEATRTSM AIRYLLLPYY YTLLHESHTT GLPILRAFSW
760 770 780 790 800
QFPNDRSLSG VDNQFFVGDG LVVTPVLEPG VDKVKGVFPG AGKEEVYYDW
810 820 830 840 850
YTQREVHFKD GKNETLDAPL GHIPLHIRGG NVLPTQEPGY TVAESRQNPF
860 870 880 890 900
GLIVALDNDG KAQGSLYLDD GESLVVDSSL LVSFSVSDNT LSASPSGDYK
910 920 930 940 950
ADQPLANVTI LGVGHKPKSV KFENANVDFT YKKSTVFVTG LDKYTKDGAF

SKDFTITW
Length:958
Mass (Da):106,508
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:i47938DB9BC308260
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
M60207 Genomic DNA Translation: AAA33923.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JN0102

<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
M60207 Genomic DNA Translation: AAA33923.1
PIRiJN0102

3D structure databases

SMRiP22861
ModBaseiSearch...

Protein family/group databases

CAZyiGH31, Glycoside Hydrolase Family 31
CLAEiGLA31A_DEBOC

Family and domain databases

Gene3Di2.60.40.1180, 2 hits
InterProiView protein in InterPro
IPR031727, Gal_mutarotase_N
IPR011013, Gal_mutarotase_sf_dom
IPR000322, Glyco_hydro_31
IPR030458, Glyco_hydro_31_AS
IPR030459, Glyco_hydro_31_CS
IPR013780, Glyco_hydro_b
IPR017853, Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF01055, Glyco_hydro_31, 1 hit
PF16863, NtCtMGAM_N, 1 hit
SUPFAMiSSF51445, SSF51445, 1 hit
SSF74650, SSF74650, 1 hit
PROSITEiView protein in PROSITE
PS00129, GLYCOSYL_HYDROL_F31_1, 1 hit
PS00707, GLYCOSYL_HYDROL_F31_2, 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 nameiAMYG_SCHOC
<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: P22861
Secondary accession number(s): Q92336
<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%5Fand%5Fisoforms">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: June 17, 2020
This is version 71 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

Direct protein sequencing

Documents

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