Annotations: 6OJO

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6ojoa_	Alpha and beta proteins (a+b)	T-fold	Tetrahydrobiopterin biosynthesis enzymes-like	automated matches	automated matches	(Yersinia pestis ) [TaxId: 632 ],	SCOPe (2.08)
B	d6ojob_	Alpha and beta proteins (a+b)	T-fold	Tetrahydrobiopterin biosynthesis enzymes-like	automated matches	automated matches	(Yersinia pestis ) [TaxId: 632 ],	SCOPe (2.08)
C	d6ojoc_	Alpha and beta proteins (a+b)	T-fold	Tetrahydrobiopterin biosynthesis enzymes-like	automated matches	automated matches	(Yersinia pestis ) [TaxId: 632 ],	SCOPe (2.08)
D	d6ojod_	Alpha and beta proteins (a+b)	T-fold	Tetrahydrobiopterin biosynthesis enzymes-like	automated matches	automated matches	(Yersinia pestis ) [TaxId: 632 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Tetrahydrobiopterin biosynthesis enzymes-like	8101305	3000283	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Tetrahydrobiopterin biosynthesis enzymes-like	8101305	3000283	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Tetrahydrobiopterin biosynthesis enzymes-like	8101305	3000283	SCOP2B (2022-06-29)
D	SCOP2 Family	DHN aldolase/epimerase	8101304	4001721	SCOP2 (2022-06-29)
D	SCOP2 Superfamily	Tetrahydrobiopterin biosynthesis enzymes-like	8101305	3000283	SCOP2 (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	FolB	e6ojoA1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: FolB	ECOD (1.6)
B	FolB	e6ojoB1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: FolB	ECOD (1.6)
C	FolB	e6ojoC1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: FolB	ECOD (1.6)
D	FolB	e6ojoD1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: FolB	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.1130.10	Alpha Beta	2-Layer Sandwich	GTP Cyclohydrolase I, domain 2	GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain	CATH (utative)
B	3.30.1130.10	Alpha Beta	2-Layer Sandwich	GTP Cyclohydrolase I, domain 2	GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain	CATH (utative)
C	3.30.1130.10	Alpha Beta	2-Layer Sandwich	GTP Cyclohydrolase I, domain 2	GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain	CATH (utative)
D	3.30.1130.10	Alpha Beta	2-Layer Sandwich	GTP Cyclohydrolase I, domain 2	GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF02152	Dihydroneopterin aldolase (FolB)	Dihydroneopterin aldolase	This enzyme EC:4.1.2.25 catalyses the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin in the biosynthetic pathway of tetrahydrofolate.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	7,8-dihydroneopterin aldolase	dihydroneopterin aldolase activity lyase activity catalytic activity carbon-carbon lyase activity aldehyde-lyase activity	oxoacid metabolic process cellular 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 oxoacid metabolic process cellular 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 cellular metabolic process dicarboxylic acid metabolic process carboxylic acid metabolic process amide biosynthetic process cellular modified amino acid metabolic process vitamin metabolic process biosynthetic process cellular modified amino acid 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	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR006156	Dihydroneopterin aldolase	Family
A, B, C, D	IPR006157	Dihydroneopterin aldolase/epimerase domain	Domain
A, B, C, D	IPR043133	GTP cyclohydrolase I, C-terminal/NADPH-dependent 7-cyano-7-deazaguanine reductase	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.