Annotations: 1AJ0

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1aj0a_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Dihydropteroate synthetase-like	Dihydropteroate synthetase	Dihydropteroate synthetase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Dihydropteroate synthetase-like	8043864	3000643	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	Pterin_bind	e1aj0A1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Pterin_bind	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.20	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Dihydropteroate synthase-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00809	Pterin binding enzyme (Pterin_bind)	Pterin binding enzyme	This family includes a variety of pterin binding enzymes that all adopt a TIM barrel fold. The family includes dihydropteroate synthase EC:2.5.1.15 as well as a group methyltransferase enzymes including methyltetrahydrofolate, corrinoid iron-sulfur p ...	This family includes a variety of pterin binding enzymes that all adopt a TIM barrel fold. The family includes dihydropteroate synthase EC:2.5.1.15 as well as a group methyltransferase enzymes including methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) Swiss:Q46389 that catalyses a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation. It transfers the N5-methyl group from methyltetrahydrofolate (CH3-H4folate) to a cob(I)amide centre in another protein, the corrinoid iron-sulfur protein. MeTr is a member of a family of proteins that includes methionine synthase and methanogenic enzymes that activate the methyl group of methyltetra-hydromethano(or -sarcino)pterin [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	DIHYDROPTEROATE SYNTHASE	dihydropteroate synthase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity cation binding ion binding binding metal ion binding small molecule binding	response to stimulus response to chemical response to xenobiotic stimulus oxoacid metabolic process modified amino acid biosynthetic process vitamin biosynthetic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process small molecule metabolic process amide metabolic process water-soluble vitamin metabolic process folic acid metabolic process dicarboxylic acid biosynthetic process response to stimulus response to chemical response to xenobiotic stimulus oxoacid metabolic process modified amino acid biosynthetic process vitamin biosynthetic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process small molecule metabolic process amide metabolic process water-soluble vitamin metabolic process folic acid metabolic process dicarboxylic acid biosynthetic process folic acid biosynthetic process folic acid-containing compound biosynthetic process water-soluble vitamin biosynthetic process small molecule biosynthetic process dicarboxylic acid metabolic process modified amino acid metabolic process carboxylic acid metabolic process amide biosynthetic process vitamin metabolic process biosynthetic process folic acid-containing compound metabolic process pteridine-containing compound biosynthetic process metabolic process cellular process pteridine-containing compound metabolic process tetrahydrofolate biosynthetic process tetrahydrofolate metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR011005	Dihydropteroate synthase-like superfamily	Homologous Superfamily
A	IPR045031	Dihydropteroate synthase-like	Family
A	IPR006390	Dihydropteroate synthase domain	Domain
A	IPR000489	Pterin-binding domain	Domain

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

Chains	Enzyme Name	Description	Catalytic Residues
A	dihydropteroate synthase M-CSA #394	Dihydropteroate synthase (DHPS) is essential for the de novo synthesis of folate in prokaryotes, in lower eukaryotes such as protozoa and yeast, and in plants. DHPS is absent in mammals. This makes it an ideal drug target.	Defined by 2 residues: LYS:A-221ARG:A-255 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.5.1.15 (PDB Primary Data) Search M-CSA Motif + EC 2.5.1.15

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.