EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR009251 Alpha-2,3-sialyltransferase

Protein matches Help

UniProtKB

Matches:

77 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR009251 A-2_3-sialyltransferase

Type

Family

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.90.1480.10	A-2_3-sialyltransferase	58
Pfam	PF06002	CST-I	62
SuperFamily	SSF102414	A-2_3-sialyltransferase	66
Signatures in BioMart

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents several alpha-2,3-sialyltransferase (EC:2.4.99) proteins, most of which are found in the food-borne pathogen Campylobacter jejuni. Sialyltransferases transfer a sialic acid moiety from cytidine-5'-monophospho-N-acetyl-neuraminic acid (CMP-NeuAc) to terminal positions of various key glycoconjugates, which play critical roles in cell recognition and adherence [1]. The structure of Cst-II alpha-2,3-sialyltransferase from C. jejuni consists of a 3-layer alpha/beta/alpha topology. Cst-II catalytic mechanism involves an essential histidine (general base) and two tyrosine residues (coordination of the phosphate leaving group) to carry out substrate binding and glycosyl transfer.

Structural links Help

PDB - click here

SCOP: c.130.1.1

CATH: 3.90.1480.10

Database links Help

PANDIT: PF06002

Taxonomic coverage Help

Example proteins Help

P24324 Uncharacterized protein HI0352

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR009251	Alpha-2,3-sialyltransferase
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Chiu CP, Watts AG, Lairson LL, Gilbert M, Lim D, Wakarchuk WW, Withers SG, Strynadka NC. Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analog. Nat. Struct. Mol. Biol. 11 163-70 2004 [PubMed: 14730352] http://dx.doi.org/10.1038/nsmb720

Additional Reading Open in usermanual
	Wang PG. The charged sialic acid exhibits its power again: a new high-throughput screening technology. Nat. Methods 3 2006 589-90 [PubMed: 16862130] http://dx.doi.org/10.1038/nmeth0806-589
	Gilbert M, Brisson JR, Karwaski MF, Michniewicz J, Cunningham AM, Wu Y, Young NM, Wakarchuk WW. Biosynthesis of ganglioside mimics in Campylobacter jejuni OH4384. Identification of the glycosyltransferase genes, enzymatic synthesis of model compounds, and characterization of nanomole amounts by 600-mhz (1)h and (13)c NMR analysis. J. Biol. Chem. 275 2000 3896-906 [PubMed: 10660542] http://dx.doi.org/10.1074/jbc.275.6.3896
	Chiu CP, Lairson LL, Gilbert M, Wakarchuk WW, Withers SG, Strynadka NC. Structural analysis of the alpha-2,3-sialyltransferase Cst-I from Campylobacter jejuni in apo and substrate-analogue bound forms. Biochemistry 46 2007 7196-204 [PubMed: 17518445] http://dx.doi.org/10.1021/bi602543d

InterPro 23.1