6WM5

Structure of a phosphatidylinositol-phosphate synthase (PIPS) from Mycobacterium kansasii

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
Membrane Protein Annotation: OPM
Membrane Protein Annotation: PDBTM

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	DIPPS domain-like	8100847	4007695	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	DIPPS domain-like	8100848	3002413	SCOP2 (2022-06-29)
A	SCOP2B Superfamily	Nucleotide-diphospho-sugar transferases	8090044	3000077	SCOP2B (2022-06-29)
B [auth C]	SCOP2B Superfamily	Nucleotide-diphospho-sugar transferases	8090044	3000077	SCOP2B (2022-06-29)
B [auth C]	SCOP2B Superfamily	DIPPS domain-like	8100848	3002413	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	CDP-OH_P_transf	e6wm5A2	A: alpha bundles	X: CDP-alcohol phosphotransferase helical bundle domain (From Topology)	H: CDP-alcohol phosphotransferase helical bundle domain (From Topology)	T: CDP-alcohol phosphotransferase helical bundle domain	F: CDP-OH_P_transf	ECOD (1.6)
B [auth C]	CDP-OH_P_transf	e6wm5C2	A: alpha bundles	X: CDP-alcohol phosphotransferase helical bundle domain (From Topology)	H: CDP-alcohol phosphotransferase helical bundle domain (From Topology)	T: CDP-alcohol phosphotransferase helical bundle domain	F: CDP-OH_P_transf	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.550.30	Alpha Beta	Alpha-Beta Complex	Spore Coat Polysaccharide Biosynthesis Protein SpsA	Chain A	CATH (utative)
A	1.20.120.1760	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	CDP-alcohol phosphotransferase transmembrane (TM) domain	CATH (utative)
B [auth C]	3.90.550.30	Alpha Beta	Alpha-Beta Complex	Spore Coat Polysaccharide Biosynthesis Protein SpsA	Chain A	CATH (utative)
B [auth C]	1.20.120.1760	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	CDP-alcohol phosphotransferase transmembrane (TM) domain	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B [auth C]	PF21682	CDP-alcohol phosphatidyltransferase AF_2299-like, N-terminal (AF_2299-like_N)	CDP-alcohol phosphatidyltransferase AF_2299-like, N-terminal	This domain is found at the N-terminal end of CDP-alcohol phosphatidyltransferase family protein from Archaeoglobus fulgidus (AF_2299) and similar archaeal proteins. AF_2299 is a member of a family of membrane-embedded enzymes known as CDP-alcohol ph ...	This domain is found at the N-terminal end of CDP-alcohol phosphatidyltransferase family protein from Archaeoglobus fulgidus (AF_2299) and similar archaeal proteins. AF_2299 is a member of a family of membrane-embedded enzymes known as CDP-alcohol phosphotransferases (CDP-APs) involved in the formation of polar phospholipids. This integral membrane phosphotransferase is organised into two distinct domains. This entry represents the N-terminal cytoplasmic domain, which has structural similarity to the cytidyltransferases [1-3].	Domain
A, B [auth C]	PF01066	CDP-alcohol phosphatidyltransferase (CDP-OH_P_transf)	CDP-alcohol phosphatidyltransferase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B [auth C]	AfCTD-Phosphatidylinositol-phosphate synthase (PIPS) fusion	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding transferase activity catalytic activity phosphotransferase activity, for other substituted phosphate groups transferase activity, transferring phosphorus-containing groups nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding	lipid biosynthetic process primary metabolic process phospholipid biosynthetic process phospholipid metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic process lipid metabolic process	cell periphery cellular anatomical structure plasma membrane membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B [auth C]	IPR043130	CDP-alcohol phosphatidyltransferase, transmembrane domain	Homologous Superfamily
A, B [auth C]	IPR044268	Phosphatidylinositol phosphate synthase PgsA1	Family
A, B [auth C]	IPR048254	CDP-alcohol phosphatidyltransferase, conserved site	Conserved Site
A, B [auth C]	IPR000462	CDP-alcohol phosphatidyltransferase	Family
A, B [auth C]	IPR043130	CDP-alcohol phosphatidyltransferase, transmembrane domain	Homologous Superfamily
A, B [auth C]	IPR049037	CDP-alcohol phosphatidyltransferase AF_2299-like, N-terminal domain	Domain
A, B [auth C]	IPR048254	CDP-alcohol phosphatidyltransferase, conserved site	Conserved Site
A, B [auth C]	IPR000462	CDP-alcohol phosphatidyltransferase	Family

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B [auth C]	OPM	Transmembrane	Alpha-helical polytopic	Choline/ethanolamine phosphotransferase	Choline/ethanolamine phosphotransferase 1

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A, B [auth C]	PDBTM	Annotated as membrane protein by PDBTM

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.