1VHQ

Crystal structure of enhancing lycopene biosynthesis protein 2

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1vhqb_	Alpha and beta proteins (a/b)	Flavodoxin-like	Class I glutamine amidotransferase-like	DJ-1/PfpI	Putative sigma cross-reacting protein 27A (SCRP-27A, EllB)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1vhqa_	Alpha and beta proteins (a/b)	Flavodoxin-like	Class I glutamine amidotransferase-like	DJ-1/PfpI	Putative sigma cross-reacting protein 27A (SCRP-27A, EllB)	(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)
B	SCOP2B Superfamily	Class I glutamine amidotransferase-like	8035831	3001405	SCOP2B (2022-06-29)
A	SCOP2 Family	DJ-1/PfpI	8023451	4003749	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Class I glutamine amidotransferase-like	8035831	3001405	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)
B	DJ-1_PfpI	e1vhqB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Class I glutamine amidotransferase-like	F: DJ-1_PfpI	ECOD (1.6)
A	DJ-1_PfpI	e1vhqA1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Class I glutamine amidotransferase-like	F: DJ-1_PfpI	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.50.880	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Class I glutamine amidotransferase (GATase) domain	CATH (4.3.0)
A	3.40.50.880	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Class I glutamine amidotransferase (GATase) domain	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Enhancing lycopene biosynthesis protein 2	lyase activity catalytic activity	biosynthetic process isoprenoid biosynthetic process lipid biosynthetic process primary metabolic process metabolic process cellular process lipid metabolic process isoprenoid metabolic process regulation of biological process regulation of cellular process regulation of lipid metabolic process biological regulation positive regulation of biological process regulation of primary metabolic process biosynthetic process isoprenoid biosynthetic process lipid biosynthetic process primary metabolic process metabolic process cellular process lipid metabolic process isoprenoid metabolic process regulation of biological process regulation of cellular process regulation of lipid metabolic process biological regulation positive regulation of biological process regulation of primary metabolic process positive regulation of isoprenoid metabolic process positive regulation of metabolic process positive regulation of lipid metabolic process regulation of isoprenoid metabolic process regulation of metabolic process positive regulation of cellular process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR029062	Class I glutamine amidotransferase-like	Homologous Superfamily
A, B	IPR026041	Glyoxalase ElbB	Family

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B	CSO	Parent Component: CYS RESID: AA0205 PSI-MOD : L-cysteine sulfenic acid MOD:00210
A, B	MSE	Parent Component: MET RESID: AA0205

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.