2AF7

Crystal structure of the gamma-carboxymuconolactone decarboxylase from Methanobacterium thermoautotrophicum. Northeast Structural Genomics Consortium target TT747.

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	d2af7a1	All alpha proteins	AhpD-like	AhpD-like	CMD-like	Gamma-carboxymuconolactone decarboxylase, CMD	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
B	d2af7b_	All alpha proteins	AhpD-like	AhpD-like	CMD-like	Gamma-carboxymuconolactone decarboxylase, CMD	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
C	d2af7c_	All alpha proteins	AhpD-like	AhpD-like	CMD-like	Gamma-carboxymuconolactone decarboxylase, CMD	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
D	d2af7d_	All alpha proteins	AhpD-like	AhpD-like	CMD-like	Gamma-carboxymuconolactone decarboxylase, CMD	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
E	d2af7e_	All alpha proteins	AhpD-like	AhpD-like	CMD-like	Gamma-carboxymuconolactone decarboxylase, CMD	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
F	d2af7f_	All alpha proteins	AhpD-like	AhpD-like	CMD-like	Gamma-carboxymuconolactone decarboxylase, CMD	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
G	d2af7g_	All alpha proteins	AhpD-like	AhpD-like	CMD-like	Gamma-carboxymuconolactone decarboxylase, CMD	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
H	d2af7h_	All alpha proteins	AhpD-like	AhpD-like	CMD-like	Gamma-carboxymuconolactone decarboxylase, CMD	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)
I	d2af7i_	All alpha proteins	AhpD-like	AhpD-like	CMD-like	Gamma-carboxymuconolactone decarboxylase, CMD	(Methanothermobacter thermautotrophicus ) [TaxId: 145262 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	CMD-like	8024587	4000771	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	AhpD-like	8036966	3001907	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	AhpD-like	8036966	3001907	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	AhpD-like	8036966	3001907	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	AhpD-like	8036966	3001907	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	AhpD-like	8036966	3001907	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	AhpD-like	8036966	3001907	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	AhpD-like	8036966	3001907	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	AhpD-like	8036966	3001907	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	AhpD-like	8036966	3001907	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	CMD	e2af7A1	A: alpha arrays	X: AhpD-like (From Topology)	H: AhpD-like (From Topology)	T: AhpD-like	F: CMD	ECOD (1.6)
B	CMD	e2af7B1	A: alpha arrays	X: AhpD-like (From Topology)	H: AhpD-like (From Topology)	T: AhpD-like	F: CMD	ECOD (1.6)
C	CMD	e2af7C1	A: alpha arrays	X: AhpD-like (From Topology)	H: AhpD-like (From Topology)	T: AhpD-like	F: CMD	ECOD (1.6)
D	CMD	e2af7D1	A: alpha arrays	X: AhpD-like (From Topology)	H: AhpD-like (From Topology)	T: AhpD-like	F: CMD	ECOD (1.6)
E	CMD	e2af7E1	A: alpha arrays	X: AhpD-like (From Topology)	H: AhpD-like (From Topology)	T: AhpD-like	F: CMD	ECOD (1.6)
F	CMD	e2af7F1	A: alpha arrays	X: AhpD-like (From Topology)	H: AhpD-like (From Topology)	T: AhpD-like	F: CMD	ECOD (1.6)
G	CMD	e2af7G1	A: alpha arrays	X: AhpD-like (From Topology)	H: AhpD-like (From Topology)	T: AhpD-like	F: CMD	ECOD (1.6)
H	CMD	e2af7H1	A: alpha arrays	X: AhpD-like (From Topology)	H: AhpD-like (From Topology)	T: AhpD-like	F: CMD	ECOD (1.6)
I	CMD	e2af7I1	A: alpha arrays	X: AhpD-like (From Topology)	H: AhpD-like (From Topology)	T: AhpD-like	F: CMD	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.20.1290.10	Mainly Alpha	Up-down Bundle	AhpD-like	AhpD-like	CATH (4.3.0)
B	1.20.1290.10	Mainly Alpha	Up-down Bundle	AhpD-like	AhpD-like	CATH (4.3.0)
C	1.20.1290.10	Mainly Alpha	Up-down Bundle	AhpD-like	AhpD-like	CATH (4.3.0)
D	1.20.1290.10	Mainly Alpha	Up-down Bundle	AhpD-like	AhpD-like	CATH (4.3.0)
E	1.20.1290.10	Mainly Alpha	Up-down Bundle	AhpD-like	AhpD-like	CATH (4.3.0)
F	1.20.1290.10	Mainly Alpha	Up-down Bundle	AhpD-like	AhpD-like	CATH (4.3.0)
G	1.20.1290.10	Mainly Alpha	Up-down Bundle	AhpD-like	AhpD-like	CATH (4.3.0)
H	1.20.1290.10	Mainly Alpha	Up-down Bundle	AhpD-like	AhpD-like	CATH (4.3.0)
I	1.20.1290.10	Mainly Alpha	Up-down Bundle	AhpD-like	AhpD-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H, I	PF02627	Carboxymuconolactone decarboxylase family (CMD)	Carboxymuconolactone decarboxylase family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H, I	gamma-carboxymuconolactone decarboxylase	peroxidase activity oxidoreductase activity antioxidant activity oxidoreductase activity, acting on peroxide as acceptor catalytic activity peroxiredoxin activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR003779	Carboxymuconolactone decarboxylase-like	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR029032	AhpD-like	Homologous Superfamily

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.