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Entry version 103 (26 Feb 2020)
Sequence version 1 (01 Feb 1997)
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Protein

N-acetyllactosaminide alpha-2,3-sialyltransferase

Gene

lst

Organism
Neisseria meningitidis serogroup B (strain MC58)
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 transfer of sialic acid from the substrate CMP-N-acetylneuraminate to the terminal galactose residue of the lacto-N-neotetraose branch of surface lipooligosaccharide (LOS), forming an alpha-2,3-sialyl linkage. Thus, functions in the sialylation of LOS, which plays a role in the evasion of the host immune response by protecting N.meningitidis from complement-mediated serum killing and from phagocytic killing by neutrophils. In vitro, can use a number of different synthetic acceptors with lactose or galactose as the saccharide portion, but shows a strong preference for the N-acetyllactosamine containing acceptor.1 Publication

Miscellaneous

Present in outer membrane vesicle formulations which are used as vaccines in human.2 Publications

<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

<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>pH dependencei

Optimum pH is 6.0.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: lipooligosaccharide biosynthesis

This protein is involved in the pathway lipooligosaccharide biosynthesis, which is part of Bacterial outer membrane biogenesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway lipooligosaccharide biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei255CMP-N-acetylneuraminate; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1
<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 sitei258Proton acceptor1 Publication1
Active sitei280Proton donor1 Publication1

<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
Biological processLipopolysaccharide biosynthesis

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
NMEN122586:G1G1B-901-MONOMER

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00501

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GT52 Glycosyltransferase Family 52

<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:
N-acetyllactosaminide alpha-2,3-sialyltransferase1 Publication (EC:2.4.99.61 Publication)
Alternative name(s):
CMP-N-acetylneuraminate:beta-galactoside alpha-2,3-sialyltransferase1 Publication
Short name:
CMP-Neu5Ac:beta-galactoside alpha-2,3-sialyltransferase1 Publication
Lipooligosaccharide sialyltransferase2 Publications
Short name:
LOS sialyltransferase2 Publications
<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:lst1 Publication
Ordered Locus Names:NMB0922
<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>OrganismiNeisseria meningitidis serogroup B (strain MC58)
<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 identifieri122586 [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 lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000425 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 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

Cell outer membrane, Membrane

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi124E → A: Decreases the binding affinity for the donor substrate (but not catalytic rate). 1 Publication1
Mutagenesisi258D → N: Loss of catalytic activity. 1 Publication1
Mutagenesisi280H → A: Decreases the rate of sialic acid transfer. 1 Publication1
Mutagenesisi282R → A: Decreases both the binding affinity for the donor substrate and the rate of sialic acid transfer. 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_00000805741 – 371N-acetyllactosaminide alpha-2,3-sialyltransferaseAdd BLAST371

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P72097

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication

<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

1371
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
P72097

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
P72097

<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>Regioni278 – 282CMP-N-acetylneuraminate bindingCombined sources1 Publication5
Regioni299 – 300CMP-N-acetylneuraminate bindingCombined sources1 Publication2
Regioni322 – 323CMP-N-acetylneuraminate bindingCombined sources1 Publication2

<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 52 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105P7J Bacteria
ENOG4111XG2 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_076077_0_0_4

KEGG Orthology (KO)

More...
KOi
K00785

Identification of Orthologs from Complete Genome Data

More...
OMAi
CCTPLQV

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR012477 Glyco_transf_52

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07922 Glyco_transf_52, 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.

P72097-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGLKKACLTV LCLIVFCFGI FYTFDRVNQG ERNAVSLLKE KLFNEEGEPV
60 70 80 90 100
NLIFCYTILQ MKVAERIMAQ HPGERFYVVL MSENRNEKYD YYFNQIKDKA
110 120 130 140 150
ERAYFFHLPY GLNKSFNFIP TMAELKVKSM LLPKVKRIYL ASLEKVSIAA
160 170 180 190 200
FLSTYPDAEI KTFDDGTGNL IQSSSYLGDE FSVNGTIKRN FARMMIGDWS
210 220 230 240 250
IAKTRNASDE HYTIFKGLKN IMDDGRRKMT YLPLFDASEL KTGDETGGTV
260 270 280 290 300
RILLGSPDKE MKEISEKAAK NFKIQYVAPH PRQTYGLSGV TTLNSPYVIE
310 320 330 340 350
DYILREIKKN PHTRYEIYTF FSGAALTMKD FPNVHVYALK PASLPEDYWL
360 370
KPVYALFTQS GIPILTFDDK N
Length:371
Mass (Da):42,611
Last modified:February 1, 1997 - 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:i1C0E51DA3DAACD15
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti2G → S in strain: M982B / NRCC 4725. 1
Natural varianti29Q → H in strain: 406Y / NRCC 4030 and NRCC 4725. 1
Natural varianti40E → D in strain: 406Y / NRCC 4030, M982B / NRCC 4725 and 126E / NRCC 4010. 1
Natural varianti94N → K in strain: 406Y / NRCC 4030 and M982B / NRCC 4725. 1
Natural varianti102R → W in strain: 126E / NRCC 4010. 1
Natural varianti129S → A in strain: 126E / NRCC 4010. 1
Natural varianti168G → I in strain: 126E / NRCC 4010. 1
Natural varianti242T → A in strain: 406Y / NRCC 4030 and 126E / NRCC 4010. 1
Natural varianti273K → N in strain: 406Y / NRCC 4030 and 126E / NRCC 4010. 1

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
U60660 Genomic DNA Translation: AAC44541.1
U60661 Genomic DNA Translation: AAC44543.1
U60662 Genomic DNA Translation: AAC44544.2
U60663 Genomic DNA Translation: AAC44545.1
AE002098 Genomic DNA Translation: AAF41330.1

Protein sequence database of the Protein Information Resource

More...
PIRi
D81143

NCBI Reference Sequences

More...
RefSeqi
NP_273962.1, NC_003112.2
WP_002244089.1, NC_003112.2

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAF41330; AAF41330; NMB0922

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
903043

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
nme:NMB0922

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|122586.8.peg.1159

<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
U60660 Genomic DNA Translation: AAC44541.1
U60661 Genomic DNA Translation: AAC44543.1
U60662 Genomic DNA Translation: AAC44544.2
U60663 Genomic DNA Translation: AAC44545.1
AE002098 Genomic DNA Translation: AAF41330.1
PIRiD81143
RefSeqiNP_273962.1, NC_003112.2
WP_002244089.1, NC_003112.2

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
2YK4X-ray1.94A49-370[»]
2YK5X-ray2.32A49-370[»]
2YK6X-ray2.83A49-370[»]
2YK7X-ray2.18A49-370[»]
SMRiP72097
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

CAZyiGT52 Glycosyltransferase Family 52

Proteomic databases

PaxDbiP72097

Genome annotation databases

EnsemblBacteriaiAAF41330; AAF41330; NMB0922
GeneIDi903043
KEGGinme:NMB0922
PATRICifig|122586.8.peg.1159

Phylogenomic databases

eggNOGiENOG4105P7J Bacteria
ENOG4111XG2 LUCA
HOGENOMiCLU_076077_0_0_4
KOiK00785
OMAiCCTPLQV

Enzyme and pathway databases

UniPathwayiUPA00501
BioCyciNMEN122586:G1G1B-901-MONOMER

Miscellaneous databases

EvolutionaryTraceiP72097

Family and domain databases

InterProiView protein in InterPro
IPR012477 Glyco_transf_52
PfamiView protein in Pfam
PF07922 Glyco_transf_52, 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 nameiLST_NEIMB
<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: P72097
Secondary accession number(s): P72099, P72100, P72101
<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: June 1, 2001
Last sequence update: February 1, 1997
Last modified: February 26, 2020
This is version 103 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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