1JYL | pdb_00001jyl

Catalytic Mechanism of CTP:phosphocholine Cytidylyltransferase from Streptococcus pneumoniae (LicC)

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1jyla1	Alpha and beta proteins (a/b)	Nucleotide-diphospho-sugar transferases	Nucleotide-diphospho-sugar transferases	Cytidylytransferase	CTP:phosphocholine cytidylytransferase LicC	(Streptococcus pneumoniae ) [TaxId: 1313 ],	SCOPe (2.08)
A	d1jyla2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Streptococcus pneumoniae ) [TaxId: 1313 ],	SCOPe (2.08)
B	d1jylb1	Alpha and beta proteins (a/b)	Nucleotide-diphospho-sugar transferases	Nucleotide-diphospho-sugar transferases	Cytidylytransferase	CTP:phosphocholine cytidylytransferase LicC	(Streptococcus pneumoniae ) [TaxId: 1313 ],	SCOPe (2.08)
B	d1jylb2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Streptococcus pneumoniae ) [TaxId: 1313 ],	SCOPe (2.08)
C	d1jylc1	Alpha and beta proteins (a/b)	Nucleotide-diphospho-sugar transferases	Nucleotide-diphospho-sugar transferases	Cytidylytransferase	CTP:phosphocholine cytidylytransferase LicC	(Streptococcus pneumoniae ) [TaxId: 1313 ],	SCOPe (2.08)
C	d1jylc2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Streptococcus pneumoniae ) [TaxId: 1313 ],	SCOPe (2.08)
D	d1jyld1	Alpha and beta proteins (a/b)	Nucleotide-diphospho-sugar transferases	Nucleotide-diphospho-sugar transferases	Cytidylytransferase	CTP:phosphocholine cytidylytransferase LicC	(Streptococcus pneumoniae ) [TaxId: 1313 ],	SCOPe (2.08)
D	d1jyld2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Streptococcus pneumoniae ) [TaxId: 1313 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	NTP_transferase	e1jylA1	A: a/b three-layered sandwiches	X: Nucleotide-diphospho-sugar transferases (From Topology)	H: Nucleotide-diphospho-sugar transferases (From Topology)	T: Nucleotide-diphospho-sugar transferases	F: NTP_transferase	ECOD (1.6)
B	NTP_transferase	e1jylB1	A: a/b three-layered sandwiches	X: Nucleotide-diphospho-sugar transferases (From Topology)	H: Nucleotide-diphospho-sugar transferases (From Topology)	T: Nucleotide-diphospho-sugar transferases	F: NTP_transferase	ECOD (1.6)
C	NTP_transferase	e1jylC1	A: a/b three-layered sandwiches	X: Nucleotide-diphospho-sugar transferases (From Topology)	H: Nucleotide-diphospho-sugar transferases (From Topology)	T: Nucleotide-diphospho-sugar transferases	F: NTP_transferase	ECOD (1.6)
D	NTP_transferase	e1jylD1	A: a/b three-layered sandwiches	X: Nucleotide-diphospho-sugar transferases (From Topology)	H: Nucleotide-diphospho-sugar transferases (From Topology)	T: Nucleotide-diphospho-sugar transferases	F: NTP_transferase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.550.10	Alpha Beta	Alpha-Beta Complex	Spore Coat Polysaccharide Biosynthesis Protein SpsA	Chain A	CATH (4.3.0)
B	3.90.550.10	Alpha Beta	Alpha-Beta Complex	Spore Coat Polysaccharide Biosynthesis Protein SpsA	Chain A	CATH (4.3.0)
C	3.90.550.10	Alpha Beta	Alpha-Beta Complex	Spore Coat Polysaccharide Biosynthesis Protein SpsA	Chain A	CATH (4.3.0)
D	3.90.550.10	Alpha Beta	Alpha-Beta Complex	Spore Coat Polysaccharide Biosynthesis Protein SpsA	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00483	Nucleotidyl transferase (NTP_transferase)	Nucleotidyl transferase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	CTP:phosphocholine Cytidylyltransferase	transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups	cellular component organization cell wall organization or biogenesis cell wall organization cellular process cellular component organization or biogenesis external encapsulating structure organization carbohydrate derivative biosynthetic process teichoic acid biosynthetic process peptidoglycan-based cell wall biogenesis small molecule biosynthetic process lipoteichoic acid metabolic process carbohydrate derivative metabolic process organic acid biosynthetic process organic acid metabolic process cellular component organization cell wall organization or biogenesis cell wall organization cellular process cellular component organization or biogenesis external encapsulating structure organization carbohydrate derivative biosynthetic process teichoic acid biosynthetic process peptidoglycan-based cell wall biogenesis small molecule biosynthetic process lipoteichoic acid metabolic process carbohydrate derivative metabolic process organic acid biosynthetic process organic acid metabolic process macromolecule biosynthetic process cellular component biogenesis cell wall biogenesis biosynthetic process cell wall macromolecule biosynthetic process lipoteichoic acid biosynthetic process metabolic process small molecule metabolic process macromolecule metabolic process teichoic acid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR050065	Bifunctional protein GlmU-like	Family
A, B, C, D	IPR017189	CTP:phosphocholine cytidylyltransferase	Family
A, B, C, D	IPR005835	Nucleotidyl transferase domain	Domain
A, B, C, D	IPR029044	Nucleotide-diphospho-sugar transferases	Homologous Superfamily

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.