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Entry version 96 (16 Oct 2019)
Sequence version 1 (01 May 1999)
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Protein

Amylosucrase

Gene

ams

Organism
Neisseria polysaccharea
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

Catalyzes the synthesis of alpha-glucan from sucrose. Catalyzes, in addition, sucrose hydrolysis, maltose and maltotriose synthesis by successive transfers of the glucosyl moiety of sucrose onto the released glucose, and finally turanose and trehalulose synthesis, these two sucrose isomers being obtained by glucosyl transfer onto fructose.1 Publication

Miscellaneous

Like the recombinant protein expressed in E.coli, the amylosucrase may be secreted in N.polysaccharea without cleavage of a signal sequence.

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Amylosucrase favors hydrolysis at low sucrose concentrations, and polymerization at high sucrose concentrations. Competitively inhibited by fructose.

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

This enzyme does not present a classic Michaelis-Menten behavior for sucrose consumption, that could be related to the presence of a second sucrose binding site. Nevertheless, it is possible to model sucrose consumption rate versus sucrose concentration by two different Michaelis-Menten equations whose apparent kinetic constants are given just above.
  1. KM=1.9 mM for sucrose (in the sucrose consumption assay, when initial sucrose < 20 mM)1 Publication
  2. KM=1.7 mM for sucrose (in the sucrose hydrolysis reaction, when initial sucrose < 20 mM)1 Publication
  3. KM=1.9 mM for sucrose (in the polymerization reaction, when initial sucrose < 20 mM)1 Publication
  4. KM=50.2 mM for sucrose (in the sucrose consumption assay, when initial sucrose > 20 mM)1 Publication
  5. KM=38.7 mM for sucrose (in the sucrose hydrolysis reaction, when initial sucrose > 20 mM)1 Publication
  1. Vmax=470 µmol/min/g enzyme for sucrose consumption (when initial sucrose < 20 mM)1 Publication
  2. Vmax=288 µmol/min/g enzyme for sucrose hydrolysis (when initial sucrose < 20 mM)1 Publication
  3. Vmax=147 µmol/min/g enzyme for polymerization reaction (when initial sucrose < 20 mM)1 Publication
  4. Vmax=1100 µmol/min/g enzyme for sucrose consumption (when initial sucrose > 20 mM)1 Publication
  5. Vmax=472 µmol/min/g enzyme for sucrose hydrolysis (when initial sucrose > 20 mM)1 Publication
  6. Vmax=1620 µmol/min/g enzyme for polymerization reaction (when initial sucrose > 20 mM)1 Publication

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 sitei152Substrate3 Publications1
Binding sitei195Substrate3 Publications1
Binding sitei262Substrate3 Publications1
Binding sitei292Substrate3 Publications1
<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 sitei294Nucleophile1 Publication1 Publication1
Active sitei336Proton donor1 Publication1
Binding sitei400Substrate3 Publications1
Binding sitei401Substrate3 Publications1
<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>Sitei452Transition state stabilizerBy similarity1
Binding sitei517Substrate3 Publications1

<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 functionGlycosyltransferase, Transferase

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.1.4 3596

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q9ZEU2

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
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:
Amylosucrase (EC:2.4.1.42 Publications)
<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:ams
<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>OrganismiNeisseria polysaccharea
<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 identifieri489 [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 lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

<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

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi195H → Q: 98% reduction of activity. 1 Publication1
Mutagenesisi294D → E or N: Complete loss of activity. 1 Publication1
Mutagenesisi308E → Q: No effect. 1 Publication1
Mutagenesisi336E → Q: Complete loss of activity. 1 Publication1
Mutagenesisi352E → Q: 30% reduction of activity. 1 Publication1
Mutagenesisi400H → N: 97% reduction of activity. 1 Publication1
Mutagenesisi401D → E: Almost complete loss of activity. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB04447 1,4-Dithiothreitol
DB02379 Beta-D-Glucose
DB02772 Sucrose

<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_00000451541 – 636AmylosucraseAdd BLAST636

<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.

4 Publications

<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

1636
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q9ZEU2

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9ZEU2

<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 13 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4107QW3 Bacteria
COG0366 LUCA

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.1180, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00128 Alpha-amylase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00642 Aamy, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51445 SSF51445, 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.

Q9ZEU2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLTPTQQVGL ILQYLKTRIL DIYTPEQRAG IEKSEDWRQF SRRMDTHFPK
60 70 80 90 100
LMNELDSVYG NNEALLPMLE MLLAQAWQSY SQRNSSLKDI DIARENNPDW
110 120 130 140 150
ILSNKQVGGV CYVDLFAGDL KGLKDKIPYF QELGLTYLHL MPLFKCPEGK
160 170 180 190 200
SDGGYAVSSY RDVNPALGTI GDLREVIAAL HEAGISAVVD FIFNHTSNEH
210 220 230 240 250
EWAQRCAAGD PLFDNFYYIF PDRRMPDQYD RTLREIFPDQ HPGGFSQLED
260 270 280 290 300
GRWVWTTFNS FQWDLNYSNP WVFRAMAGEM LFLANLGVDI LRMDAVAFIW
310 320 330 340 350
KQMGTSCENL PQAHALIRAF NAVMRIAAPA VFFKSEAIVH PDQVVQYIGQ
360 370 380 390 400
DECQIGYNPL QMALLWNTLA TREVNLLHQA LTYRHNLPEH TAWVNYVRSH
410 420 430 440 450
DDIGWTFADE DAAYLGISGY DHRQFLNRFF VNRFDGSFAR GVPFQYNPST
460 470 480 490 500
GDCRVSGTAA ALVGLAQDDP HAVDRIKLLY SIALSTGGLP LIYLGDEVGT
510 520 530 540 550
LNDDDWSQDS NKSDDSRWAH RPRYNEALYA QRNDPSTAAG QIYQGLRHMI
560 570 580 590 600
AVRQSNPRFD GGRLVTFNTN NKHIIGYIRN NALLAFGNFS EYPQTVTAHT
610 620 630
LQAMPFKAHD LIGGKTVSLN QDLTLQPYQV MWLEIA
Length:636
Mass (Da):72,344
Last modified:May 1, 1999 - 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:iB7656C19BF1A2065
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence described in PubMed:9150231 differs from that shown. Reason: Frameshift.Curated

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 conflicti14Y → H in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti84 – 85NS → SA in AAM51153 (PubMed:12517860).Curated2
Sequence conflicti89D → N in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti93A → E in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti159S → T AA sequence (PubMed:9150231).Curated1
Sequence conflicti171G → D in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti208Missing AA sequence (PubMed:9150231).Curated1
Sequence conflicti392A → S in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti437S → T AA sequence (PubMed:9150231).Curated1
Sequence conflicti449S → N in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti459A → S in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti463V → A in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti468D → N in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti474D → S in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti501L → P in AAM51153 (PubMed:12517860).Curated1
Sequence conflicti505 – 510DWSQDS → GWAQDG in AAM51153 (PubMed:12517860).Curated6

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
AJ011781 Genomic DNA Translation: CAA09772.1
AY099335 Genomic DNA Translation: AAM51153.1

NCBI Reference Sequences

More...
RefSeqi
WP_003751803.1, NZ_CP031325.1

<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
AJ011781 Genomic DNA Translation: CAA09772.1
AY099335 Genomic DNA Translation: AAM51153.1
RefSeqiWP_003751803.1, NZ_CP031325.1

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
1G5AX-ray1.40A13-636[»]
1JG9X-ray1.66A13-636[»]
1JGIX-ray2.00A13-636[»]
1MVYX-ray2.00A13-636[»]
1MW0X-ray2.01A13-636[»]
1MW1X-ray2.10A13-636[»]
1MW2X-ray2.10A13-636[»]
1MW3X-ray2.00A13-636[»]
1S46X-ray2.20A13-636[»]
1ZS2X-ray2.16A13-636[»]
3UEQX-ray1.85A13-636[»]
4FLOX-ray2.20A13-636[»]
4FLQX-ray2.50A13-636[»]
4FLRX-ray2.40A13-636[»]
4FLSX-ray2.30A13-636[»]
5N6VX-ray1.60A13-636[»]
5N7JX-ray2.00A13-636[»]
SMRiQ9ZEU2
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

DrugBankiDB04447 1,4-Dithiothreitol
DB02379 Beta-D-Glucose
DB02772 Sucrose

Protein family/group databases

CAZyiGH13 Glycoside Hydrolase Family 13

Phylogenomic databases

eggNOGiENOG4107QW3 Bacteria
COG0366 LUCA

Enzyme and pathway databases

BRENDAi2.4.1.4 3596
SABIO-RKiQ9ZEU2

Miscellaneous databases

EvolutionaryTraceiQ9ZEU2

Family and domain databases

Gene3Di2.60.40.1180, 1 hit
InterProiView protein in InterPro
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00128 Alpha-amylase, 1 hit
SMARTiView protein in SMART
SM00642 Aamy, 1 hit
SUPFAMiSSF51445 SSF51445, 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 nameiAMYS_NEIPO
<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: Q9ZEU2
Secondary accession number(s): Q84HD5
<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: December 20, 2005
Last sequence update: May 1, 1999
Last modified: October 16, 2019
This is version 96 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 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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