P72074 (LST_NEIGO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase
Short name=Alpha 2,3-ST
Short name=Beta-galactoside alpha-2,3-sialyltransferase
EC=2.4.99.-

Alternative name(s):
Lipooligosaccharide sialyltransferase

Gene names

Name:

lst

Organism

Neisseria gonorrhoeae

Taxonomic identifier

485 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	371 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	Lipopolysaccharide biosynthesis
Molecular function	Glycosyltransferase Transferase
Gene Ontology (GO)
Biological process	lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	transferase activity, transferring glycosyl groups Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 371	371	CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase		PRO_0000080572

Sequences

	Sequence		Length	Mass (Da)
	P72074 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: C197AD342E87F461	FASTA	371	42,682
	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

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
EMBL GenBank DDBJ	U60664 Genomic DNA. Translation: AAC44539.1.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT52. Glycosyltransferase Family 52.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR012477. Glyco_transf_52. [Graphical view]
Pfam	PF07922. Glyco_transf_52. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LST_NEIGO

Accession

Primary (citable) accession number: P72074

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	February 1, 1997
Last modified:	January 11, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program