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Protein

Glucoamylase 1

Gene
N/A
Organism
Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
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

Miscellaneous

Rhizopus glucoamylase exists in multiple forms, Gluc 1, Gluc 2, and Gluc 3, all of which hydrolyze gelatinized starch at similar rates, but only the largest one (Gluc 1) is able to adsorb raw starch.
Glucoamylase 3 may be 110-604 instead of 116-104.

<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 ‘Function’ 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 sitei279SubstrateBy similarity1
<p>This subsection of the ‘Function’ 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 sitei336Proton acceptorPROSITE-ProRule annotation1
Active sitei339Proton 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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.3 5365

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
CBM21 Carbohydrate-Binding Module Family 21
GH15 Glycoside Hydrolase Family 15

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

More...
mycoCLAPi
GLA15E_RHIOR

<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 1 (EC:3.2.1.3)
Short name:
Gluc 1
Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase
Cleaved into the following 2 chains:
Glucoamylase 2
Short name:
Gluc 2
Glucoamylase 3
Short name:
Gluc 3
<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>OrganismiRhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
<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 identifieri64495 [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 lineageiEukaryotaFungiFungi incertae sedisMucoromycotaMucoromycotinaMucoromycetesMucoralesMucorineaeRhizopodaceaeRhizopus

<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
CHEMBL4449

<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 – 25Add BLAST25
<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_000000147226 – 604Glucoamylase 1Add BLAST579
ChainiPRO_0000001473116 – 604Glucoamylase 3Add BLAST489
ChainiPRO_0000001474159 – 604Glucoamylase 2Add BLAST446

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>Glycosylationi122N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi167N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi230N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi236N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi564N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P07683

<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

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P07683

<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

Secondary structure

1604
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P07683

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

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SMRi
P07683

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P07683

<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>Domaini26 – 130CBM21PROSITE-ProRule annotationAdd BLAST105

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni26 – 115Adsorption to raw starchAdd BLAST90
Regioni116 – 604Starch degradationAdd BLAST489

<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

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.50.10.10, 1 hit
2.60.40.2440, 2 hits

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
IPR005036 CBM21_dom
IPR038175 CBM21_dom_sf
IPR011613 GH15-like
IPR000165 Glucoamylase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03370 CBM_21, 1 hit
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
PS51159 CBM21, 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>.<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.

P07683-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQLFNLPLKV SFFLVLSYFS LLVSAASIPS SASVQLDSYN YDGSTFSGKI
60 70 80 90 100
YVKNIAYSKK VTVIYADGSD NWNNNGNTIA ASYSAPISGS NYEYWTFSAS
110 120 130 140 150
INGIKEFYIK YEVSGKTYYD NNNSANYQVS TSKPTTTTAT ATTTTAPSTS
160 170 180 190 200
TTTPPSRSEP ATFPTGNSTI SSWIKKQEGI SRFAMLRNIN PPGSATGFIA
210 220 230 240 250
ASLSTAGPDY YYAWTRDAAL TSNVIVYEYN TTLSGNKTIL NVLKDYVTFS
260 270 280 290 300
VKTQSTSTVC NCLGEPKFNP DASGYTGAWG RPQNDGPAER ATTFILFADS
310 320 330 340 350
YLTQTKDASY VTGTLKPAIF KDLDYVVNVW SNGCFDLWEE VNGVHFYTLM
360 370 380 390 400
VMRKGLLLGA DFAKRNGDST RASTYSSTAS TIANKISSFW VSSNNWIQVS
410 420 430 440 450
QSVTGGVSKK GLDVSTLLAA NLGSVDDGFF TPGSEKILAT AVAVEDSFAS
460 470 480 490 500
LYPINKNLPS YLGNSIGRYP EDTYNGNGNS QGNSWFLAVT GYAELYYRAI
510 520 530 540 550
KEWIGNGGVT VSSISLPFFK KFDSSATSGK KYTVGTSDFN NLAQNIALAA
560 570 580 590 600
DRFLSTVQLH AHNNGSLAEE FDRTTGLSTG ARDLTWSHAS LITASYAKAG

APAA
Length:604
Mass (Da):65,162
Last modified:November 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:i78421F1AAA93ADB9
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
D00049 Genomic DNA Translation: BAA00033.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JP0001

<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
D00049 Genomic DNA Translation: BAA00033.1
PIRiJP0001

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DJMNMR-A26-131[»]
ProteinModelPortaliP07683
SMRiP07683
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP07683
ChEMBLiCHEMBL4449

Protein family/group databases

CAZyiCBM21 Carbohydrate-Binding Module Family 21
GH15 Glycoside Hydrolase Family 15
mycoCLAPiGLA15E_RHIOR

Proteomic databases

PRIDEiP07683

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.3 5365

Miscellaneous databases

EvolutionaryTraceiP07683

Family and domain databases

Gene3Di1.50.10.10, 1 hit
2.60.40.2440, 2 hits
InterProiView protein in InterPro
IPR008928 6-hairpin_glycosidase_sf
IPR012341 6hp_glycosidase-like_sf
IPR005036 CBM21_dom
IPR038175 CBM21_dom_sf
IPR011613 GH15-like
IPR000165 Glucoamylase
PfamiView protein in Pfam
PF03370 CBM_21, 1 hit
PF00723 Glyco_hydro_15, 1 hit
PRINTSiPR00736 GLHYDRLASE15
SUPFAMiSSF48208 SSF48208, 1 hit
PROSITEiView protein in PROSITE
PS51159 CBM21, 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_RHIOR
<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: P07683
<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: April 1, 1988
Last sequence update: November 1, 1995
Last modified: December 5, 2018
This is version 110 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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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