4EXQ

CRYSTAL STRUCTURE of UROPORPHYRINOGEN DECARBOXYLASE (UPD) FROM BURKHOLDERIA THAILANDENSIS E264

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	d4exqa1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	UROD/MetE-like	Uroporphyrinogen decarboxylase, UROD	automated matches	(Burkholderia thailandensis E264 ) [TaxId: 271848 ],	SCOPe (2.08)
A	d4exqa2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Burkholderia thailandensis E264 ) [TaxId: 271848 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Uroporphyrinogen decarboxylase, UROD	8072662	4003345	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	UROD/MetE-like	8072663	3000657	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	URO-D	e4exqA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: URO-D	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.210	Alpha Beta	Alpha-Beta Barrel	TIM Barrel		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01208	Uroporphyrinogen decarboxylase (URO-D) (URO-D)	Uroporphyrinogen decarboxylase (URO-D)	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Uroporphyrinogen decarboxylase	uroporphyrinogen decarboxylase activity carboxy-lyase activity lyase activity catalytic activity carbon-carbon lyase activity	pigment metabolic process heme metabolic process porphyrin-containing compound biosynthetic process heme biosynthetic process oxoacid metabolic process protoporphyrinogen IX metabolic process pigment biosynthetic process amino acid metabolic process organic acid metabolic process alpha-amino acid metabolic process glutamine family amino acid metabolic process tetrapyrrole biosynthetic process from glutamate tetrapyrrole biosynthetic process glutamate metabolic process pigment metabolic process heme metabolic process porphyrin-containing compound biosynthetic process heme biosynthetic process oxoacid metabolic process protoporphyrinogen IX metabolic process pigment biosynthetic process amino acid metabolic process organic acid metabolic process alpha-amino acid metabolic process glutamine family amino acid metabolic process tetrapyrrole biosynthetic process from glutamate tetrapyrrole biosynthetic process glutamate metabolic process small molecule metabolic process porphyrin-containing compound metabolic process protoporphyrinogen IX biosynthetic process from glutamate tetrapyrrole metabolic process dicarboxylic acid metabolic process carboxylic acid metabolic process primary metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process protoporphyrinogen IX biosynthetic process biosynthetic process metabolic process cellular process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR006361	Uroporphyrinogen decarboxylase HemE	Family
A	IPR038071	UROD/MetE-like superfamily	Homologous Superfamily
A	IPR000257	Uroporphyrinogen decarboxylase (URO-D)	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.