4R83

Crystal structure of Sialyltransferase from Photobacterium damsela

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Type B glycosyltransferase-like	8085117	3001586	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Type B glycosyltransferase-like	8085117	3001586	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Type B glycosyltransferase-like	8085117	3001586	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Type B glycosyltransferase-like	8085117	3001586	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	PKD_4	e4r83A1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PKD_4	ECOD (1.6)
A	PM0188_C	e4r83A3	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: PM0188_C	ECOD (1.6)
A	PM0188_N	e4r83A2	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: PM0188_N	ECOD (1.6)
B	PKD_4	e4r83B1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PKD_4	ECOD (1.6)
B	PM0188_C	e4r83B3	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: PM0188_C	ECOD (1.6)
B	PM0188_N	e4r83B2	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: PM0188_N	ECOD (1.6)
C	PKD_4	e4r83C1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PKD_4	ECOD (1.6)
C	PM0188_C	e4r83C2	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: PM0188_C	ECOD (1.6)
C	PM0188_N	e4r83C3	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: PM0188_N	ECOD (1.6)
D	PKD_4	e4r83D2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PKD_4	ECOD (1.6)
D	PM0188_C	e4r83D4	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: PM0188_C	ECOD (1.6)
D	PM0188_N	e4r83D3	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: PM0188_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.3010	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
A	3.40.50.11120	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Sialyltransferase, N-terminal GT-B Rossman nucleotide-binding domain	CATH (4.3.0)
A	3.40.50.11110	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Sialyltransferase, C-terminal GT-B Rossman nucleotide-binding domain	CATH (4.3.0)
B	2.60.40.3010	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
B	3.40.50.11120	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Sialyltransferase, N-terminal GT-B Rossman nucleotide-binding domain	CATH (4.3.0)
B	3.40.50.11110	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Sialyltransferase, C-terminal GT-B Rossman nucleotide-binding domain	CATH (4.3.0)
C	2.60.40.3010	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
C	3.40.50.11120	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Sialyltransferase, N-terminal GT-B Rossman nucleotide-binding domain	CATH (4.3.0)
C	3.40.50.11110	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Sialyltransferase, C-terminal GT-B Rossman nucleotide-binding domain	CATH (4.3.0)
D	2.60.40.3010	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
D	3.40.50.11120	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Sialyltransferase, N-terminal GT-B Rossman nucleotide-binding domain	CATH (4.3.0)
D	3.40.50.11110	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Sialyltransferase, C-terminal GT-B Rossman nucleotide-binding domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF11477	Sialyltransferase PMO188 (PM0188)	Sialyltransferase PMO188	-	Family
A, B, C, D	PF22352	K319L-like, PKD domain (K319L-like_PKD)	K319L-like, PKD domain	This entry represents the PKD domain of Dyslexia-associated protein KIAA0319-like protein, in which it is found in four copies. This entry also includes Kunitz-type protease inhibitor 1 and LRP11 from human.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Sialyltransferase 0160	glycosyltransferase activity transferase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding	phosphate ion homeostasis intracellular phosphate ion homeostasis cellular homeostasis inorganic ion homeostasis chemical homeostasis homeostatic process intracellular chemical homeostasis localization transport phosphate ion transport establishment of localization inorganic anion transport regulation of biological process regulation of cellular process phosphate ion homeostasis intracellular phosphate ion homeostasis cellular homeostasis inorganic ion homeostasis chemical homeostasis homeostatic process intracellular chemical homeostasis localization transport phosphate ion transport establishment of localization inorganic anion transport regulation of biological process regulation of cellular process cellular metabolic process negative regulation of metabolic process biological regulation negative regulation of biological process negative regulation of phosphate metabolic process regulation of cellular metabolic process negative regulation of cellular metabolic process regulation of phosphate metabolic process phosphate-containing compound metabolic process negative regulation of phosphorus metabolic process negative regulation of cellular process regulation of phosphorus metabolic process metabolic process cellular process phosphorus metabolic process regulation of metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR038078	PhoU-like domain superfamily	Homologous Superfamily
A, B, C, D	IPR026022	PhoU domain	Domain
A, B, C, D	IPR021574	Sialyltransferase PMO188	Family
A, B, C, D	IPR028366	Phosphate transport system protein PhoU	Family
A, B, C, D	IPR043078	Sialyltransferase, N-terminal GT-B Rossman nucleotide-binding domain	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.