Annotations: 2WML

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Sialyltransferase/TPK catalytic domain-like	8053225	3000683	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Glyco_transf_29	e2wmlA1	A: a/b three-layered sandwiches	X: Alpha-2,3/8-sialyltransferase CstII-related (From Topology)	H: Alpha-2,3/8-sialyltransferase CstII-related (From Topology)	T: Alpha-2,3/8-sialyltransferase CstII-related	F: Glyco_transf_29	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.1480.20	Alpha Beta	Alpha-Beta Complex	sialyltransferase cstii, chain A	Glycosyl transferase family 29	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00777	Glycosyltransferase family 29 (sialyltransferase) (Glyco_transf_29)	Glycosyltransferase family 29 (sialyltransferase)	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	CMP-N-ACETYLNEURAMINATE-BETA-GALACTOSAMIDE -ALPHA-2\,3-SIALYLTRANSFERASE	beta-galactoside (CMP) alpha-2,3-sialyltransferase activity glycosyltransferase activity sialyltransferase activity transferase activity catalytic activity beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminide alpha-2,3- sialyltransferase	carbohydrate derivative biosynthetic process cellular biosynthetic process cellular metabolic process glycoprotein biosynthetic process carbohydrate derivative metabolic process primary metabolic process glycoprotein metabolic process protein N-linked glycosylation protein glycosylation macromolecule biosynthetic process biosynthetic process glycosylation macromolecule modification macromolecule glycosylation carbohydrate derivative biosynthetic process cellular biosynthetic process cellular metabolic process glycoprotein biosynthetic process carbohydrate derivative metabolic process primary metabolic process glycoprotein metabolic process protein N-linked glycosylation protein glycosylation macromolecule biosynthetic process biosynthetic process glycosylation macromolecule modification macromolecule glycosylation metabolic process cellular process protein metabolic process macromolecule metabolic process protein modification process oxoacid metabolic process carboxylic acid metabolic process organic acid metabolic process amino sugar metabolic process small molecule metabolic process amide metabolic process N-acetylneuraminate metabolic process sphingolipid biosynthetic process glycolipid metabolic process lipid biosynthetic process ganglioside biosynthetic process ceramide metabolic process membrane lipid metabolic process glycosphingolipid metabolic process liposaccharide metabolic process amide biosynthetic process sphingolipid metabolic process glycolipid biosynthetic process ceramide biosynthetic process cellular lipid metabolic process glycosphingolipid biosynthetic process ganglioside biosynthetic process via lactosylceramide membrane lipid biosynthetic process ganglioside metabolic process lipid metabolic process sialylation	membrane-bounded organelle Golgi trans cisterna intracellular anatomical structure Golgi cisterna membrane Golgi apparatus subcompartment Golgi apparatus organelle subcompartment Golgi trans cisterna membrane membrane Golgi cisterna cellular anatomical entity intracellular membrane-bounded organelle endomembrane system intracellular organelle membrane-bounded organelle Golgi trans cisterna intracellular anatomical structure Golgi cisterna membrane Golgi apparatus subcompartment Golgi apparatus organelle subcompartment Golgi trans cisterna membrane membrane Golgi cisterna cellular anatomical entity intracellular membrane-bounded organelle endomembrane system intracellular organelle organelle Golgi stack cytoplasm organelle membrane extracellular region trans-Golgi network membrane trans-Golgi network Golgi medial cisterna membrane Golgi medial cisterna

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR051757	Beta-galactoside alpha2-3 sialyltransferases	Family
A	IPR012163	Sialyltransferase	Family
A	IPR001675	Glycosyl transferase family 29	Family
A	IPR038578	GT29-like superfamiliy	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	beta-galactoside alpha-2,3-sialyltransferase M-CSA #340	Glycosyltransferase enzymes perform the sialyation of glycojonguates, molecules which have vital roles in cell recognition, adhesion and immunogenicity. The subset of sialyl-transferases (ST) catalyse the transfer of the sialic acid moiety from a cytidine-5'-monophosphate-N-acyl neuraminic acid donor to various acceptor glyco-conjuates terminating in either galactose, N-acetyl-galactosamine or another sialic acid. The enzyme annotated here, ST3Gal-I, catalyses the displacement reaction between CMP-N-acetylneuraminate and beta-D-Galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl and is a member of the glycosyl transferase family 29. Bacterial sialytransferase enzymes contain a DXD domain which binds two divalent cations that are essential for catalysis. No such domain is present in the mammalian homologues, and the activity of these enzymes is found not to be dependent upon the presence of metal cofactors [PMID:19820709]. While the glycosyltransferase-catalysed reactions had been assumed to be uni-directional, the narrow difference in favourability for glycoside formation has been exploited to synthesise rare NDP-sugar products [PMID:16946071].	Defined by 2 residues: TYR:A-224 [auth A-269]HIS:A-274 [auth A-319] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.4.99.4 (PDB Primary Data) Search M-CSA Motif + EC 2.4.99.4 EC: 2.4.3.4 (UniProt) Search M-CSA Motif + EC 2.4.3.4 EC: 2.4.3.2 (UniProt) Search M-CSA Motif + EC 2.4.3.2

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.