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Reviewed, UniProtKB/Swiss-Prot P72074 (LST_NEIGO)

Last modified June 16, 2009. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase
      Short name=Beta-galactoside alpha-2,3-sialyltransferase
      Short name=Alpha 2,3-ST
    EC=2.4.99.-
Alternative name(s):
    Lipooligosaccharide sialyltransferase
Gene names
Name: lst
OrganismNeisseria gonorrhoeae
Taxonomic identifier485 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length371 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Transfers sialic acid from the substrate CMP-sialic acid donor to the terminal beta-D-galactosyl-1,4-acetyl-beta-D-glucosamine on the lacto-N-neotetraose branch of the lipooligosaccharide.

Catalytic activity

CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-acetyl-beta-D-glucosamine = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine.

Pathway

Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.

Sequence similarities

Belongs to the glycosyltransferase 52 family.

Ontologies

Keywords
   Biological processLipopolysaccharide biosynthesis
   Molecular functionGlycosyltransferase
Transferase
Gene Ontology (GO)
   Biological processlipopolysaccharide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionsialyltransferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 371371CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase
PRO_0000080572

Sequences

Sequence LengthMass (Da)Tools
P72074-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: C197AD342E87F461

FASTA37142,682
        10         20         30         40         50         60 
MGLKKVCLTV LCLIVFCFGI FYTFDRVNQG ERNAVSLLKD KLFNEEGKPV NLIFCYTILQ 

        70         80         90        100        110        120 
MKVAERIMAQ HPGERFYVVL MSENRNEKYD YYFNQIKDKA ERAYFFYLPY GLNKSFNFIP 

       130        140        150        160        170        180 
TMAELKVKSM LLPKVKRIYL ASLEKVSIAA FLSTYPDAEI KTFDDGTNNL IRESSYLGGE 

       190        200        210        220        230        240 
FAVNGAIKRN FARMMVGDWS IAKTRNASDE HYTIFKGLKN IMDDGRRKMT YLPLFDASEL 

       250        260        270        280        290        300 
KAGDETGGTV RILLGSPDKE MKEISEKAAK NFNIQYVAPH PRQTYGLSGV TALNSPYVIE 

       310        320        330        340        350        360 
DYILREIKKN PHTRYEIYTF FSGAALTMKD FPNVHVYALK PASLPEDYWL KPVYALFRQA 

       370 
DIPILTFDDK N 

« Hide

References

[1]"Cloning of the lipooligosaccharide alpha-2,3-sialyltransferase from the bacterial pathogens Neisseria meningitidis and Neisseria gonorrhoeae."
Gilbert M., Watson D.C., Cunningham A.-M., Jennings M.P., Young N.M., Wakarchuk W.W.
J. Biol. Chem. 271:28271-28276(1996) [PubMed: 8910446] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 33084 / F62 / M-1914.

Cross-references

Sequence databases

U60664 Genomic DNA. Translation: AAC44539.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGT52. Glycosyltransferase Family 52.

Family and domain databases

InterProIPR012477. Glyco_transf_52.
[Graphical view]
PfamPF07922. Glyco_transf_52. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLST_NEIGO
AccessionPrimary (citable) accession number: P72074
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: February 1, 1997
Last modified: June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents