Annotations: 1DCO

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1dcoa_	Alpha and beta proteins (a+b)	DCoH-like	PCD-like	PCD-like	Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
B	d1dcob_	Alpha and beta proteins (a+b)	DCoH-like	PCD-like	PCD-like	Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
C	d1dcoc_	Alpha and beta proteins (a+b)	DCoH-like	PCD-like	PCD-like	Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
D	d1dcod_	Alpha and beta proteins (a+b)	DCoH-like	PCD-like	PCD-like	Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
E	d1dcoe_	Alpha and beta proteins (a+b)	DCoH-like	PCD-like	PCD-like	Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
F	d1dcof_	Alpha and beta proteins (a+b)	DCoH-like	PCD-like	PCD-like	Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
H	d1dcoh_	Alpha and beta proteins (a+b)	DCoH-like	PCD-like	PCD-like	Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
G	d1dcog_	Alpha and beta proteins (a+b)	DCoH-like	PCD-like	PCD-like	Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	PCD-like	8035863	3001639	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	PCD-like	8035863	3001639	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	PCD-like	8035863	3001639	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	PCD-like	8035863	3001639	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	PCD-like	8035863	3001639	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	PCD-like	8035863	3001639	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	PCD-like	8035863	3001639	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	PCD-like	8035863	3001639	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_4a	e1dcoA1	A: a+b two layers	X: DCoH-like	H: Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) (From Topology)	T: Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH)	F: Pterin_4a	ECOD (1.6)
B	Pterin_4a	e1dcoB1	A: a+b two layers	X: DCoH-like	H: Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) (From Topology)	T: Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH)	F: Pterin_4a	ECOD (1.6)
C	Pterin_4a	e1dcoC1	A: a+b two layers	X: DCoH-like	H: Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) (From Topology)	T: Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH)	F: Pterin_4a	ECOD (1.6)
D	Pterin_4a	e1dcoD1	A: a+b two layers	X: DCoH-like	H: Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) (From Topology)	T: Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH)	F: Pterin_4a	ECOD (1.6)
E	Pterin_4a	e1dcoE1	A: a+b two layers	X: DCoH-like	H: Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) (From Topology)	T: Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH)	F: Pterin_4a	ECOD (1.6)
F	Pterin_4a	e1dcoF1	A: a+b two layers	X: DCoH-like	H: Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) (From Topology)	T: Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH)	F: Pterin_4a	ECOD (1.6)
H	Pterin_4a	e1dcoH1	A: a+b two layers	X: DCoH-like	H: Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) (From Topology)	T: Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH)	F: Pterin_4a	ECOD (1.6)
G	Pterin_4a	e1dcoG1	A: a+b two layers	X: DCoH-like	H: Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) (From Topology)	T: Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH)	F: Pterin_4a	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.1360.20	Alpha Beta	2-Layer Sandwich	Gyrase A	domain 2	CATH (4.3.0)
B	3.30.1360.20	Alpha Beta	2-Layer Sandwich	Gyrase A	domain 2	CATH (4.3.0)
C	3.30.1360.20	Alpha Beta	2-Layer Sandwich	Gyrase A	domain 2	CATH (4.3.0)
D	3.30.1360.20	Alpha Beta	2-Layer Sandwich	Gyrase A	domain 2	CATH (4.3.0)
E	3.30.1360.20	Alpha Beta	2-Layer Sandwich	Gyrase A	domain 2	CATH (4.3.0)
F	3.30.1360.20	Alpha Beta	2-Layer Sandwich	Gyrase A	domain 2	CATH (4.3.0)
H	3.30.1360.20	Alpha Beta	2-Layer Sandwich	Gyrase A	domain 2	CATH (4.3.0)
G	3.30.1360.20	Alpha Beta	2-Layer Sandwich	Gyrase A	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H	PF01329	Pterin 4 alpha carbinolamine dehydratase (Pterin_4a)	Pterin 4 alpha carbinolamine dehydratase	Pterin 4 alpha carbinolamine dehydratase is also known as DCoH (dimerisation cofactor of hepatocyte nuclear factor 1-alpha).	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H	DCOH	transcription coactivator activity transcription regulator activity transcription coregulator activity protein-macromolecule adaptor activity molecular adaptor activity oxidoreductase activity monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen phenylalanine 4-monooxygenase activity catalytic activity 4-alpha-hydroxytetrahydrobiopterin dehydratase activity hydro-lyase activity lyase activity transcription coactivator activity transcription regulator activity transcription coregulator activity protein-macromolecule adaptor activity molecular adaptor activity oxidoreductase activity monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen phenylalanine 4-monooxygenase activity catalytic activity 4-alpha-hydroxytetrahydrobiopterin dehydratase activity hydro-lyase activity lyase activity carbon-oxygen lyase activity identical protein binding protein binding binding	erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process aromatic amino acid metabolic process oxoacid metabolic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process organic acid metabolic process alpha-amino acid metabolic process L-amino acid metabolic process L-phenylalanine metabolic process proteinogenic amino acid metabolic process metabolic process cellular process small molecule metabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process aromatic amino acid metabolic process oxoacid metabolic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process organic acid metabolic process alpha-amino acid metabolic process L-amino acid metabolic process L-phenylalanine metabolic process proteinogenic amino acid metabolic process metabolic process cellular process small molecule metabolic process polyol metabolic process small molecule biosynthetic process organic hydroxy compound metabolic process alcohol metabolic process diol biosynthetic process diol metabolic process biosynthetic process tetrahydrobiopterin biosynthetic process tetrahydrobiopterin metabolic process organic hydroxy compound biosynthetic process pteridine-containing compound biosynthetic process polyol biosynthetic process alcohol biosynthetic process pteridine-containing compound metabolic process regulation of protein binding regulation of molecular function regulation of binding biological regulation regulation of cellular process positive regulation of DNA-templated transcription positive regulation of biological process RNA metabolic process positive regulation of macromolecule biosynthetic process regulation of primary metabolic process nucleobase-containing compound metabolic process RNA biosynthetic process nucleic acid biosynthetic process positive regulation of metabolic process DNA-templated transcription regulation of RNA metabolic process positive regulation of biosynthetic process positive regulation of macromolecule metabolic process regulation of nucleobase-containing compound metabolic process positive regulation of cellular process regulation of RNA biosynthetic process regulation of biosynthetic process regulation of biological process positive regulation of nucleobase-containing compound metabolic process regulation of macromolecule metabolic process nucleobase-containing compound biosynthetic process gene expression macromolecule biosynthetic process nucleic acid metabolic process positive regulation of RNA metabolic process regulation of gene expression positive regulation of RNA biosynthetic process regulation of macromolecule biosynthetic process macromolecule metabolic process regulation of DNA-templated transcription regulation of metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR036428	Pterin 4 alpha carbinolamine dehydratase superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR001533	Pterin 4 alpha carbinolamine dehydratase	Family

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

Chains	Enzyme Name	Description	Catalytic Residues
A	4a-hydroxytetrahydrobiopterin dehydratase M-CSA #73	4a-Hydroxy-tetrahydrobiopterin dehydratase/DCoH is a bifunctional protein. In the cytoplasm it is an enzyme required for the regeneration of tetrahydrobiopterin, an essential cofactor for phenylalanine hydroxylase. In the nucleus it functions as a transcriptional coactivator by forming a 2:2 heterotetramer with the hepatic nuclear factor HNF1alpha (HNF1). The enzymatic catalytic form is a tetramer whereas the mode of binding to the nuclear factor is as a heterotetramer. The enzyme catalyses the dehydration of 4a-carbinolamine biopterin cofactor, a substrate used by the aromatic acid hydroxylases and NO synthase. Mutations of DcoHin humans have been associated with elevated levels of phenylalanine and the excretion of large amounts of 7-substituted pterins.	Defined by 6 residues: GLU:A-58HIS:A-62HIS:A-63HIS:A-80GLU:A-81ASP:A-89 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 4.2.1.96 (PDB Primary Data) Search M-CSA Motif + EC 4.2.1.96

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.