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Protein

Maltogenic alpha-amylase

Gene

amyM

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score:

Annotation score:5 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

Converts starch into maltose.

<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 (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains. EC:3.2.1.133

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+1 PublicationNote: Binds 3 Ca2+ ions per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi54Calcium 1Combined sources1 Publication1
Metal bindingi56Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi59Calcium 1Combined sources1 Publication1
Metal bindingi60Calcium 1Combined sources1 Publication1
Metal bindingi81Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi83Calcium 1Combined sources1 Publication1
Metal bindingi109Calcium 2Combined sources1 Publication1
Metal bindingi110Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi112Calcium 2Combined sources1 Publication1
<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 sitei126SubstrateBy similarity1
Metal bindingi134Calcium 2Combined sources1 Publication1
Metal bindingi135Calcium 2Combined sources1 Publication1
Metal bindingi164Calcium 3Combined sources1 Publication1
Binding sitei165SubstrateBy similarity1
Metal bindingi217Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi231Calcium 3Combined sources1 Publication1
Binding sitei259SubstrateBy 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 sitei261NucleophileBy similarity1
Metal bindingi265Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Active sitei289Proton donorBy similarity1
Binding sitei292Substrate; via amide nitrogenBy similarity1
Binding sitei362SubstrateBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei362Transition state stabilizerBy similarity1
Binding sitei409SubstrateBy 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
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.133 623

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
CBM20 Carbohydrate-Binding Module Family 20
GH13 Glycoside Hydrolase Family 13

<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:
Maltogenic alpha-amylase (EC:3.2.1.133)
Alternative name(s):
Glucan 1,4-alpha-maltohydrolase
<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:amyM
<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>OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
<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 identifieri1422 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Used in the food industry to prevent bread from staling. Sold under the name Novamyl by Novozymes.Curated

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB03971 Acarbose Derived Hexasaccharide
DB03323 Maltose

<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 – 331 PublicationAdd BLAST33
<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_000000142234 – 719Maltogenic alpha-amylaseAdd BLAST686

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P19531

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

<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

1719
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
P19531

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

More...
SMRi
P19531

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
P19531

<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 – 608IPT/TIGAdd BLAST77
Domaini609 – 719CBM20PROSITE-ProRule annotationAdd BLAST111

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>Regioni264 – 265Substrate bindingBy similarity2

<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 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K05992

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05820 CBM20_novamyl, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 2 hits
2.60.40.1180, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006048 A-amylase/branching_C
IPR031319 A-amylase_C
IPR006046 Alpha_amylase
IPR013784 Carb-bd-like_fold
IPR034849 CBM20_novamyl
IPR002044 CBM_fam20
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR002909 IPT_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00128 Alpha-amylase, 1 hit
PF02806 Alpha-amylase_C, 1 hit
PF00686 CBM_20, 1 hit
PF01833 TIG, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00110 ALPHAAMYLASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00642 Aamy, 1 hit
SM00632 Aamy_C, 1 hit
SM01065 CBM_2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49452 SSF49452, 1 hit
SSF51445 SSF51445, 1 hit
SSF81296 SSF81296, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51166 CBM20, 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.

P19531-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKKTLSLFV GLMLLIGLLF SGSLPYNPNA AEASSSASVK GDVIYQIIID
60 70 80 90 100
RFYDGDTTNN NPAKSYGLYD PTKSKWKMYW GGDLEGVRQK LPYLKQLGVT
110 120 130 140 150
TIWLSPVLDN LDTLAGTDNT GYHGYWTRDF KQIEEHFGNW TTFDTLVNDA
160 170 180 190 200
HQNGIKVIVD FVPNHSTPFK ANDSTFAEGG ALYNNGTYMG NYFDDATKGY
210 220 230 240 250
FHHNGDISNW DDRYEAQWKN FTDPAGFSLA DLSQENGTIA QYLTDAAVQL
260 270 280 290 300
VAHGADGLRI DAVKHFNSGF SKSLADKLYQ KKDIFLVGEW YGDDPGTANH
310 320 330 340 350
LEKVRYANNS GVNVLDFDLN TVIRNVFGTF TQTMYDLNNM VNQTGNEYKY
360 370 380 390 400
KENLITFIDN HDMSRFLSVN SNKANLHQAL AFILTSRGTP SIYYGTEQYM
410 420 430 440 450
AGGNDPYNRG MMPAFDTTTT AFKEVSTLAG LRRNNAAIQY GTTTQRWINN
460 470 480 490 500
DVYIYERKFF NDVVLVAINR NTQSSYSISG LQTALPNGSY ADYLSGLLGG
510 520 530 540 550
NGISVSNGSV ASFTLAPGAV SVWQYSTSAS APQIGSVAPN MGIPGNVVTI
560 570 580 590 600
DGKGFGTTQG TVTFGGVTAT VKSWTSNRIE VYVPNMAAGL TDVKVTAGGV
610 620 630 640 650
SSNLYSYNIL SGTQTSVVFT VKSAPPTNLG DKIYLTGNIP ELGNWSTDTS
660 670 680 690 700
GAVNNAQGPL LAPNYPDWFY VFSVPAGKTI QFKFFIKRAD GTIQWENGSN
710
HVATTPTGAT GNITVTWQN
Length:719
Mass (Da):78,676
Last modified:August 15, 2003 - 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:iB40B61AD964F7D89
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 conflicti109D → N in AAA22233 (Ref. 1) Curated1
Sequence conflicti254 – 256Missing in AAA22233 (Ref. 1) Curated3
Sequence conflicti371S → SK in AAA22233 (Ref. 1) Curated1
Sequence conflicti379 – 391ALAFI…RGTPS → RLLSFSLRGVRPP (Ref. 1) CuratedAdd BLAST13

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
M36539 Genomic DNA Translation: AAA22233.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S28784

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:AAA22233

<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
M36539 Genomic DNA Translation: AAA22233.1
PIRiS28784

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
1QHOX-ray1.70A34-719[»]
1QHPX-ray1.70A34-719[»]
ProteinModelPortaliP19531
SMRiP19531
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB03971 Acarbose Derived Hexasaccharide
DB03323 Maltose

Protein family/group databases

CAZyiCBM20 Carbohydrate-Binding Module Family 20
GH13 Glycoside Hydrolase Family 13

Proteomic databases

PRIDEiP19531

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA22233

Phylogenomic databases

KOiK05992

Enzyme and pathway databases

BRENDAi3.2.1.133 623

Miscellaneous databases

EvolutionaryTraceiP19531

Family and domain databases

CDDicd05820 CBM20_novamyl, 1 hit
Gene3Di2.60.40.10, 2 hits
2.60.40.1180, 1 hit
InterProiView protein in InterPro
IPR006048 A-amylase/branching_C
IPR031319 A-amylase_C
IPR006046 Alpha_amylase
IPR013784 Carb-bd-like_fold
IPR034849 CBM20_novamyl
IPR002044 CBM_fam20
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR002909 IPT_dom
PfamiView protein in Pfam
PF00128 Alpha-amylase, 1 hit
PF02806 Alpha-amylase_C, 1 hit
PF00686 CBM_20, 1 hit
PF01833 TIG, 1 hit
PRINTSiPR00110 ALPHAAMYLASE
SMARTiView protein in SMART
SM00642 Aamy, 1 hit
SM00632 Aamy_C, 1 hit
SM01065 CBM_2, 1 hit
SUPFAMiSSF49452 SSF49452, 1 hit
SSF51445 SSF51445, 1 hit
SSF81296 SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS51166 CBM20, 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 nameiAMYM_GEOSE
<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: P19531
<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: February 1, 1991
Last sequence update: August 15, 2003
Last modified: December 5, 2018
This is version 123 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 programProkaryotic 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, Direct protein sequencing

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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