5SVB

Mechanism of ATP-Dependent Acetone Carboxylation, Acetone Carboxylase AMP bound structure

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF02538	e5svbA3	A: beta sandwiches	X: Apc (acetophenone carboxylase) beta subunit C-terminal domain (From Topology)	H: Apc (acetophenone carboxylase) beta subunit C-terminal domain (From Topology)	T: Apc (acetophenone carboxylase) beta subunit C-terminal domain	F: PF02538	ECOD (1.6)
A	PF02538	e5svbA2	A: a+b two layers	X: MocoBD/DmpA-related (From Homology)	H: MocoBD/DmpA-related	T: Apc (acetophenone carboxylase) beta subunit middle domain	F: PF02538	ECOD (1.6)
A	PF02538	e5svbA1	A: a+b three layers	X: Profilin-like	H: N-terminal domain of Apc beta-subunit (From Topology)	T: N-terminal domain of Apc beta-subunit	F: PF02538	ECOD (1.6)
D	PF02538	e5svbD1	A: beta sandwiches	X: Apc (acetophenone carboxylase) beta subunit C-terminal domain (From Topology)	H: Apc (acetophenone carboxylase) beta subunit C-terminal domain (From Topology)	T: Apc (acetophenone carboxylase) beta subunit C-terminal domain	F: PF02538	ECOD (1.6)
D	PF02538	e5svbD2	A: a+b two layers	X: MocoBD/DmpA-related (From Homology)	H: MocoBD/DmpA-related	T: Apc (acetophenone carboxylase) beta subunit middle domain	F: PF02538	ECOD (1.6)
D	PF02538	e5svbD3	A: a+b three layers	X: Profilin-like	H: N-terminal domain of Apc beta-subunit (From Topology)	T: N-terminal domain of Apc beta-subunit	F: PF02538	ECOD (1.6)
B	PF19278	e5svbB2	A: beta sandwiches	X: beta sandwich domain in acetophenone carboxylase (Apc) alpha subunit (From Topology)	H: beta sandwich domain in acetophenone carboxylase (Apc) alpha subunit (From Topology)	T: beta sandwich domain in acetophenone carboxylase (Apc) alpha subunit	F: PF19278	ECOD (1.6)
B	PF19278	e5svbB4	A: a+b two layers	X: Reverse ferredoxin	H: a+b domain in Acetophenone carboxylase (Apc) alpha subunit (From Topology)	T: a+b domain in Acetophenone carboxylase (Apc) alpha subunit	F: PF19278	ECOD (1.6)
B	PF05378	e5svbB3	A: a/b three-layered sandwiches	X: a/b domain in Acetophenone carboxylase (Apc) alpha subunit (From Topology)	H: a/b domain in Acetophenone carboxylase (Apc) alpha subunit (From Topology)	T: a/b domain in Acetophenone carboxylase (Apc) alpha subunit	F: PF05378	ECOD (1.6)
B	PF01968	e5svbB1	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: PF01968	ECOD (1.6)
B	PF01968,PF05378	e5svbB5	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: PF01968,PF05378	ECOD (1.6)
E	PF19278	e5svbE4	A: beta sandwiches	X: beta sandwich domain in acetophenone carboxylase (Apc) alpha subunit (From Topology)	H: beta sandwich domain in acetophenone carboxylase (Apc) alpha subunit (From Topology)	T: beta sandwich domain in acetophenone carboxylase (Apc) alpha subunit	F: PF19278	ECOD (1.6)
E	PF19278	e5svbE5	A: a+b two layers	X: Reverse ferredoxin	H: a+b domain in Acetophenone carboxylase (Apc) alpha subunit (From Topology)	T: a+b domain in Acetophenone carboxylase (Apc) alpha subunit	F: PF19278	ECOD (1.6)
E	PF05378	e5svbE1	A: a/b three-layered sandwiches	X: a/b domain in Acetophenone carboxylase (Apc) alpha subunit (From Topology)	H: a/b domain in Acetophenone carboxylase (Apc) alpha subunit (From Topology)	T: a/b domain in Acetophenone carboxylase (Apc) alpha subunit	F: PF05378	ECOD (1.6)
E	PF01968	e5svbE2	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: PF01968	ECOD (1.6)
E	PF01968,PF05378	e5svbE3	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: PF01968,PF05378	ECOD (1.6)
C	PF08882	e5svbC1	A: few secondary structure elements	X: Rubredoxin-like	H: Rubredoxin-related	T: Rubredoxin-related	F: PF08882	ECOD (1.6)
F	PF08882	e5svbF1	A: few secondary structure elements	X: Rubredoxin-like	H: Rubredoxin-related	T: Rubredoxin-related	F: PF08882	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, D	PF02538	Hydantoinase B/oxoprolinase (Hydantoinase_B)	Hydantoinase B/oxoprolinase	-	Family
B, E	PF01968	Hydantoinase/oxoprolinase (Hydantoinase_A)	Hydantoinase/oxoprolinase	-	Family
B, E	PF19278	Hydantoinase/oxoprolinase C-terminal domain (Hydant_A_C)	Hydantoinase/oxoprolinase C-terminal domain	This domain is found at the C-terminus of acetophenone carboxylase alpha subunit [1]. According to ECOD this domain adopts a reverse ferredoxin fold. This domain is found at the C-terminus of a wide range of related enzymes subunits.	Domain
B, E	PF05378	Hydantoinase/oxoprolinase N-terminal region (Hydant_A_N)	Hydantoinase/oxoprolinase N-terminal region	-	Family
C, F	PF08882	Acetone carboxylase gamma subunit (Acetone_carb_G)	Acetone carboxylase gamma subunit	Acetone carboxylase is the key enzyme of bacterial acetone metabolism, catalysing the condensation of acetone and CO(2) to form acetoacetate.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, D	Acetone carboxylase alpha subunit	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding acetone carboxylase activity ligase activity, forming carbon-carbon bonds catalytic activity ligase activity hydrolase activity	cellular response to stimulus cellular detoxification cellular response to chemical stimulus response to stimulus response to chemical detoxification cellular process cellular detoxification of acetone cellular response to toxic substance response to toxic substance	-
B, E	Acetone carboxylase beta subunit	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding acetone carboxylase activity ligase activity, forming carbon-carbon bonds catalytic activity ligase activity hydrolase activity	cellular response to stimulus cellular detoxification cellular response to chemical stimulus response to stimulus response to chemical detoxification cellular process cellular detoxification of acetone cellular response to toxic substance response to toxic substance	-
C, F	Acetone carboxylase gamma subunit	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding acetone carboxylase activity ligase activity, forming carbon-carbon bonds catalytic activity ligase activity	cellular response to stimulus cellular detoxification cellular response to chemical stimulus response to stimulus response to chemical detoxification cellular process cellular detoxification of acetone cellular response to toxic substance response to toxic substance	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, D	IPR045079	Oxoprolinase family	Family
A, D	IPR003692	Hydantoinase B/oxoprolinase	Domain
B, E	IPR049517	Acetophenone carboxylase-like, C-terminal domain	Domain
B, E	IPR043129	ATPase, nucleotide binding domain	Homologous Superfamily
B, E	IPR002821	Hydantoinase A/oxoprolinase	Domain
B, E	IPR045079	Oxoprolinase family	Family
B, E	IPR008040	Hydantoinase/oxoprolinase, N-terminal	Domain
C, F	IPR016750	Acetophenone carboxylase beta subunit/Acetone carboxylase gamma subunit	Family

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 R01GM133198.