3ZGJ

S221M V223F Y359A mutant of 4-Hydroxymandelate synthase from Streptomyces coelicolor

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	HPPD_N_like	e3zgjA7	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: HPPD_N_like	ECOD (1.6)
A	Glyoxalase_10	e3zgjA4	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: Glyoxalase_10	ECOD (1.6)
A	Glyoxalase_4_2	e3zgjA6	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: Glyoxalase_4_2	ECOD (1.6)
A	Glyoxalase_5_C	e3zgjA5	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: Glyoxalase_5_C	ECOD (1.6)
B	HPPD_N_like	e3zgjB8	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: HPPD_N_like	ECOD (1.6)
B	Glyoxalase_10	e3zgjB5	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: Glyoxalase_10	ECOD (1.6)
B	Glyoxalase_4_2	e3zgjB7	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: Glyoxalase_4_2	ECOD (1.6)
B	Glyoxalase_5_C	e3zgjB6	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: Glyoxalase_5_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.180.10	Alpha Beta	Roll	2,3-Dihydroxybiphenyl 1,2-Dioxygenase	domain 1	CATH (4.3.0)
B	3.10.180.10	Alpha Beta	Roll	2,3-Dihydroxybiphenyl 1,2-Dioxygenase	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00903	Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily (Glyoxalase)	Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	4-HYDROXYPHENYLPYRUVIC ACID DIOXYGENASE	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen oxidoreductase activity 4-hydroxyphenylpyruvate dioxygenase activity oxidoreductase activity, acting on single donors with incorporation of molecular oxygen catalytic activity dioxygenase activity cation binding ion binding binding metal ion binding small molecule binding	catabolic process oxoacid metabolic process aromatic amino acid family catabolic process amino acid metabolic process organic acid catabolic process organic acid metabolic process alpha-amino acid metabolic process cellular catabolic process carboxylic acid catabolic process small molecule metabolic process tyrosine metabolic process amino acid catabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process aromatic amino acid metabolic process catabolic process oxoacid metabolic process aromatic amino acid family catabolic process amino acid metabolic process organic acid catabolic process organic acid metabolic process alpha-amino acid metabolic process cellular catabolic process carboxylic acid catabolic process small molecule metabolic process tyrosine metabolic process amino acid catabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process aromatic amino acid metabolic process carboxylic acid metabolic process L-amino acid catabolic process primary metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid catabolic process alpha-amino acid catabolic process proteinogenic amino acid catabolic process tyrosine catabolic process metabolic process cellular process small molecule catabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR005956	4-hydroxyphenylpyruvate dioxygenase	Family
A, B	IPR041736	4-hydroxyphenylpyruvate dioxygenase, N-terminal	Domain
A, B	IPR029068	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Homologous Superfamily
A, B	IPR037523	Vicinal oxygen chelate (VOC) domain	Domain
A, B	IPR004360	Glyoxalase/fosfomycin resistance/dioxygenase domain	Domain
A, B	IPR041735	4-hydroxyphenylpyruvate dioxygenase, C-terminal	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.