1UW8

CRYSTAL STRUCTURE OF OXALATE DECARBOXYLASE

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
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	d1uw8a_	All beta proteins	Double-stranded beta-helix	RmlC-like cupins	Germin/Seed storage 7S protein	Oxalate decarboxylase OxdC (YvrK)	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	RmlC-like cupins	8039833	3001825	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	Cupin_1	e1uw8A2	A: beta sandwiches	X: jelly-roll	H: Double-stranded beta-helix (From Topology)	T: Double-stranded beta-helix	F: Cupin_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.120.10	Mainly Beta	Sandwich	Jelly Rolls	Jelly Rolls	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00190	Cupin (Cupin_1)	Cupin	This family represents the conserved barrel domain of the 'cupin' superfamily [1] ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major ...	This family represents the conserved barrel domain of the 'cupin' superfamily [1] ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	OXALATE DECARBOXYLASE OXDC	oxalate decarboxylase activity carboxy-lyase activity lyase activity catalytic activity carbon-carbon lyase activity cation binding ion binding binding metal ion binding small molecule binding	organic substance metabolic process oxalate metabolic process oxoacid metabolic process cellular metabolic process dicarboxylic acid metabolic process carboxylic acid metabolic process small molecule metabolic process metabolic process cellular process organic acid metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR017774	Bicupin, oxalate decarboxylase/oxidase	Family
A	IPR006045	Cupin 1	Domain
A	IPR011051	RmlC-like cupin domain superfamily	Homologous Superfamily
A	IPR014710	RmlC-like jelly roll fold	Homologous Superfamily

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

Chains	Enzyme Name	Description	Catalytic Residues
A	oxalate decarboxylase M-CSA #231	Oxalate decarboxylase (OxdC), isolated from Bacillus subtilus, catalyses the conversion of oxalate into formate and carbon dioxide. OxdC is part of the bicupin (contain two copies of the cupin domain) subset of the cupin superfamily. The enzymes requires Mn(II) and dioxygen as cofactors. The enzyme contains two manganese binding sites but it is currently thought that only the N-terminal site I possesses catalytic activity and that the C-terminal site II is structural. However, the matter is the subject of ongoing debate. Further, this enzyme contains an unusual cofactor in the form of molecular oxygen, which is thought to act as an activator to the Mn(II) centre by increasing its redox potential.	Defined by 6 residues: ARG:A-92HIS:A-95HIS:A-97GLU:A-101HIS:A-140GLU:A-162 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 4.1.1.2 (PDB Primary Data) Search M-CSA Motif + EC 4.1.1.2

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.