1I2B

CRYSTAL STRUCTURE OF MUTANT T145A SQD1 PROTEIN COMPLEX WITH NAD AND UDP-SULFOQUINOVOSE/UDP-GLUCOSE

External Resource: Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1i2ba1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Sulfolipid biosynthesis protein SQD1	thale cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
A	d1i2ba2	Artifacts	Tags	Tags	Tags	N-terminal Tags	thale cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	SDR-like	8058104	3000038	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	GDP_Man_Dehyd	e1i2bA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: GDP_Man_Dehyd	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
A	3.90.25.10	Alpha Beta	Alpha-Beta Complex	UDP-galactose 4-epimerase	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01370	NAD dependent epimerase/dehydratase family (Epimerase)	NAD dependent epimerase/dehydratase family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	SULFOLIPID BIOSYNTHESIS PROTEIN SQD1	transferase activity, transferring sulphur-containing groups sulfotransferase activity transferase activity catalytic activity hydrolase activity UDPsulfoquinovose synthase activity hydrolase activity, acting on carbon-sulfur bonds cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding	carbohydrate derivative biosynthetic process membrane lipid metabolic process glycolipid metabolic process liposaccharide metabolic process carbohydrate derivative metabolic process lipid biosynthetic process glycolipid biosynthetic process primary metabolic process biosynthetic process metabolic process cellular process membrane lipid biosynthetic process lipid metabolic process cellular response to stimulus carbohydrate derivative biosynthetic process membrane lipid metabolic process glycolipid metabolic process liposaccharide metabolic process carbohydrate derivative metabolic process lipid biosynthetic process glycolipid biosynthetic process primary metabolic process biosynthetic process metabolic process cellular process membrane lipid biosynthetic process lipid metabolic process cellular response to stimulus cellular response to nutrient levels response to nutrient levels cellular response to phosphate starvation response to stimulus cellular response to stress response to stress response to starvation cellular response to starvation	cell periphery cellular anatomical structure plasma membrane membrane membrane-bounded organelle intracellular organelle intracellular anatomical structure plastid organelle cytoplasm intracellular membrane-bounded organelle chloroplast

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A	IPR001509	NAD-dependent epimerase/dehydratase	Domain

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.