5MSC

Structure of the A domain of carboxylic acid reductase (CAR) from Nocardia iowensis in complex with AMP

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	AMP-binding_3rd	e5mscA1	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: AMP-binding_3rd	ECOD (1.6)
A	AMP-binding_C	e5mscA4	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: AMP-binding_C	ECOD (1.6)
A	AMP-binding_1st	e5mscA3	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: AMP-binding_1st	ECOD (1.6)
A	AMP-binding_2nd	e5mscA2	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: AMP-binding_2nd	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00501	AMP-binding enzyme (AMP-binding)	AMP-binding enzyme	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Carboxylic acid reductase	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 CoA-ligase activity fatty acid ligase activity long-chain fatty acid-CoA ligase activity ligase activity, forming carbon-sulfur bonds fatty acid-CoA ligase activity catalytic activity acid-thiol ligase activity ligase activity ATP-dependent activity NADP binding vitamin binding amide binding modified amino acid binding phosphopantetheine binding oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors aldehyde dehydrogenase (NADP+) activity aryl-aldehyde dehydrogenase (NADP+) activity aldehyde dehydrogenase [NAD(P)+] activity oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor	-	cellular anatomical structure membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR009081	Phosphopantetheine binding ACP domain	Domain
A	IPR046407	Carboxylic acid reductase	Family
A	IPR020806	Polyketide synthase-like, phosphopantetheine-binding domain	Domain
A	IPR020845	AMP-binding, conserved site	Conserved Site
A	IPR013120	Fatty acyl-coenzyme A reductase-like, NAD-binding domain	Domain
A	IPR042099	ANL, N-terminal domain	Homologous Superfamily
A	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A	IPR036736	ACP-like superfamily	Homologous Superfamily
A	IPR000873	AMP-dependent synthetase/ligase domain	Domain
A	IPR010080	Thioester reductase-like domain	Domain

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.