3DGB

Crystal structure of muconate lactonizing enzyme from Pseudomonas Fluorescens complexed with muconolactone

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3dgba2	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Enolase C-terminal domain-like	automated matches	automated matches	(Pseudomonas protegens Pf-5 ) [TaxId: 220664 ],	SCOPe (2.08)
A	d3dgba1	Alpha and beta proteins (a+b)	Enolase N-terminal domain-like	Enolase N-terminal domain-like	automated matches	automated matches	(Pseudomonas protegens Pf-5 ) [TaxId: 220664 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	MR_MLE_N	e3dgbA1	A: a+b two layers	X: Enolase-N/ribosomal protein	H: Enolase N-terminal domain-like (From Topology)	T: Enolase N-terminal domain-like	F: MR_MLE_N	ECOD (1.6)
A	MR_MLE_C_1	e3dgbA2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: MR_MLE_C_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.390.10	Alpha Beta	2-Layer Sandwich	Enolase-like	domain 1	CATH (4.3.0)
A	3.20.20.120	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Enolase-like C-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF02746	Mandelate racemase / muconate lactonizing enzyme, N-terminal domain (MR_MLE_N)	Mandelate racemase / muconate lactonizing enzyme, N-terminal domain	SCOP reports fold similarity with enolase N-terminal domain.	Domain
A	PF13378	Enolase C-terminal domain-like (MR_MLE_C)	Enolase C-terminal domain-like	This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N Pfam:PF02746 domain. EC:4.2.1.40.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Muconate cycloisomerase	intramolecular lyase activity isomerase activity chloromuconate cycloisomerase activity catalytic activity cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding muconate cycloisomerase activity	catabolic process organic substance metabolic process metabolic process amino acid metabolic process primary metabolic process amino acid catabolic process organic substance catabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR029065	Enolase C-terminal domain-like	Domain
A	IPR013341	Mandelate racemase/muconate lactonizing enzyme, N-terminal domain	Domain
A	IPR018110	Mandelate racemase/muconate lactonizing enzyme, conserved site	Conserved Site
A	IPR013342	Mandelate racemase/muconate lactonizing enzyme, C-terminal	Domain
A	IPR013370	Muconate/chloromuconate cycloisomerase	Family
A	IPR029017	Enolase-like, N-terminal	Homologous Superfamily
A	IPR036849	Enolase-like, C-terminal domain superfamily	Homologous Superfamily

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

Chains	Enzyme Name	Description	Catalytic Residues
A	muconate cycloisomerase (syn) M-CSA #269	Catalyses the syn cycloisomerisation of +-muconolactone to cis-cis-muconate. Involved in the second step of the subpathway that synthesizes 5-oxo-4,5-dihydro-2-furylacetate from catechol.	Defined by 8 residues: HIS:A-24LYS:A-169LYS:A-171ASP:A-200GLU:A-226ASP:A-251LYS:A-275GLU:A-329 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 5.5.1.1 (PDB Primary Data) Search M-CSA Motif + EC 5.5.1.1

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.