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Entry version 89 (11 Dec 2019)
Sequence version 1 (01 Jun 2003)
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Protein

Sucrose synthase

Gene

ss2

Organism
Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298)
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 reversible conversion of sucrose and a nucleotide disphosphate (NDP) into fructose and NDP-glucose; although the reaction is freely reversible in vitro, the physiological reaction seems to be sucrose cleavage. Unlike characterized plant enzymes prefers ADP as a cosubstrate, whereas plants prefer UDP (PubMed:25846332, PubMed:26013491). The KM for sucrose is 8-fold lower in the presence of ADP than UDP (PubMed:25846332). Its preference for ADP over UDP suggests it may directly link sucrose and glycogen metabolism (Probable).Curated2 Publications

<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

Inhibited by GDP over 10 mM and by over 2 mM MgCl2.1 Publication

<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

  1. KM=40 mM for sucrose with ADP during sucrose degradation1 Publication
  2. KM=321 mM for sucrose with UDP during sucrose degradation1 Publication
  3. KM=0.44 mM for ADP in sucrose breakdown1 Publication
  4. KM=1.28 mM for CDP in sucrose breakdown1 Publication
  5. KM=1.56 mM for GDP in sucrose breakdown1 Publication
  6. KM=0.69 mM for UDP in sucrose breakdown1 Publication
  1. Vmax=20.8 µmol/min/mg enzyme in sucrose breakdown with ADP1 Publication
  2. Vmax=11.5 µmol/min/mg enzyme in sucrose breakdown with CDP1 Publication
  3. Vmax=40.1 µmol/min/mg enzyme in sucrose breakdown with GDP1 Publication
  4. Vmax=67.7 µmol/min/mg enzyme in sucrose breakdown with UDP1 Publication

pH dependencei

Optimum pH is 5.0.1 Publication

Temperature dependencei

Optimum temperature is 75 degrees Celsius. Retains about 55% activity after 15 minutes at 65 degrees Celsius.1 Publication

<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

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GT4 Glycosyltransferase Family 4

<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:
Sucrose synthase (EC:2.4.1.131 Publication)
Short name:
SuSyNe1 Publication
<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:ss2
Ordered Locus Names:NE1214
<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>OrganismiNitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298)
<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 identifieri228410 [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 lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas
<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
  • UP000001416 <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

<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>Mutagenesisi567R → A: 2500-fold decrease in Vmax for UDP-glucose, 2600-fold decrease for ADP-glucose. 1 Publication1
Mutagenesisi572K → A: 2200-fold decrease in Vmax for UDP-glucose, 2300-fold decrease for ADP-glucose. 1 Publication1
Mutagenesisi663E → A: 430-fold decrease in Vmax for UDP-glucose, 185-fold decrease for ADP-glucose. 1 Publication1

<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_00004422581 – 794Sucrose synthaseAdd BLAST794

<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

Homotetramer.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
228410.NE1214

<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

1794
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
Q820M5

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

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>Regioni263 – 742GT-B glycosyltransferaseBy similarityAdd BLAST480

<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 glycosyltransferase 1 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105Q84 Bacteria
ENOG410XSQT LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000240125

KEGG Orthology (KO)

More...
KOi
K00695

Identification of Orthologs from Complete Genome Data

More...
OMAi
GPLEIIQ

Database of Orthologous Groups

More...
OrthoDBi
694191at2

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001296 Glyco_trans_1
IPR000368 Sucrose_synth
IPR012820 Sucrose_synthase_pln/cyn

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00534 Glycos_transf_1, 1 hit
PF00862 Sucrose_synth, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02470 sucr_synth, 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.

Q820M5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTTIDTLATC TQQNRDAVYT LLRRYFTANR TLLLQSDLRE GLLQTEQDCG
60 70 80 90 100
QSDMLRAFVF RLQEGIFSSP WAYLALRPEI AKWEFMRIHQ EHLIPEKLTI
110 120 130 140 150
SEFLKFKETV VKGEATESVL EVDFGPFNRG FPRLKESRSI GQGVIFLNRK
160 170 180 190 200
LSSEMFSRIE AGHTSLLHFL GVHAIEGQQL MFSNNSHDIH AVRNQLRQAL
210 220 230 240 250
EMLETLDGTT PWIELAPKMN QLGFAPGWGH NANRVAETMN MLMDILEAPS
260 270 280 290 300
PSALEEFLAC IPMISRLLIL SPHGYFGQDN VLGLPDTGGQ VVYILDQVRA
310 320 330 340 350
LEKEMHDRLQ LQGVQVEPKI LIVTRLIPDA GDTTCNQRLE KVSGCTNTWI
360 370 380 390 400
LRVPFRKHNG EIIPHWISRF EIWPHLEIFA GDVEREALAE LGGHPDLIIG
410 420 430 440 450
NYSDGNLVAT LLSRRLGVTQ CNIAHALEKT KYLHSDIYWQ ENEDKYHFSC
460 470 480 490 500
QYTADLLAMN SADFIVTSTY QEIAGTREAE GQYESYQAFS MPDLYRVIHG
510 520 530 540 550
IDLFDPKFNI VSPGANADIY FPYSDPNRRL HSLIPEIESL IFDDATNLPA
560 570 580 590 600
RGYLQDPDKP LIFTMARLDR IKNITGLVEL YAASPRLRSL ANLVIVGGKI
610 620 630 640 650
DPQHSSDHEE QEQIHRMHQL MDEHELDQQV RWLGMRLDKN LAGELYRYIA
660 670 680 690 700
DKRGIFVQPA LFEAFGLTII EAMASGLPTF ATRYGGPLEI IQNNRSGFHI
710 720 730 740 750
DPNQGAATAD LIADFFEKNL ENPQEWERIS QGALDRVASR YTWKLYAERM
760 770 780 790
MTLSRIYGFW KFVSGLEREE TDRYLNMFYH LQFRPLANRL AHEI
Length:794
Mass (Da):90,865
Last modified:June 1, 2003 - 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:i3A046387F29DF2CB
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
AL954747 Genomic DNA Translation: CAD85125.1

NCBI Reference Sequences

More...
RefSeqi
WP_011111802.1, NC_004757.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAD85125; CAD85125; NE1214

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
neu:NE1214

<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
AL954747 Genomic DNA Translation: CAD85125.1
RefSeqiWP_011111802.1, NC_004757.1

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
4RBNX-ray3.05A/B/C/D1-794[»]
SMRiQ820M5
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi228410.NE1214

Protein family/group databases

CAZyiGT4 Glycosyltransferase Family 4

Genome annotation databases

EnsemblBacteriaiCAD85125; CAD85125; NE1214
KEGGineu:NE1214

Phylogenomic databases

eggNOGiENOG4105Q84 Bacteria
ENOG410XSQT LUCA
HOGENOMiHOG000240125
KOiK00695
OMAiGPLEIIQ
OrthoDBi694191at2

Family and domain databases

InterProiView protein in InterPro
IPR001296 Glyco_trans_1
IPR000368 Sucrose_synth
IPR012820 Sucrose_synthase_pln/cyn
PfamiView protein in Pfam
PF00534 Glycos_transf_1, 1 hit
PF00862 Sucrose_synth, 1 hit
TIGRFAMsiTIGR02470 sucr_synth, 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 nameiSUS_NITEU
<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: Q820M5
<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: November 22, 2017
Last sequence update: June 1, 2003
Last modified: December 11, 2019
This is version 89 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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