2BLL

Apo-structure of the C-terminal decarboxylase domain of ArnA

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	d2blla1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Polymyxin resistance protein ArnA (PrmI)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	SDR-like	8057775	3000038	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	GDP_Man_Dehyd_1	e2bllA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: GDP_Man_Dehyd_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
A	3.90.25.10	Alpha Beta	Alpha-Beta Complex	UDP-galactose 4-epimerase	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01370	NAD dependent epimerase/dehydratase family (Epimerase)	NAD dependent epimerase/dehydratase family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PROTEIN YFBG	NAD+ binding NAD binding binding nucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding heterocyclic compound binding small molecule binding oxidoreductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor NAD+ binding NAD binding binding nucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding heterocyclic compound binding small molecule binding oxidoreductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on CH-OH group of donors UDP-glucuronic acid dehydrogenase activity catalytic activity carboxy-lyase activity lyase activity carbon-carbon lyase activity UDP-glucuronate decarboxylase activity transferase activity, transferring one-carbon groups UDP-4-amino-4-deoxy-L-arabinose formyltransferase activity transferase activity hydroxymethyl-, formyl- and related transferase activity identical protein binding protein binding	glycolipid metabolic process cellular biosynthetic process lipid A biosynthetic process carbohydrate derivative metabolic process lipid biosynthetic process phospholipid metabolic process phosphate-containing compound metabolic process lipooligosaccharide biosynthetic process phosphorus metabolic process carbohydrate derivative biosynthetic process membrane lipid metabolic process lipooligosaccharide metabolic process cellular metabolic process liposaccharide metabolic process glycolipid metabolic process cellular biosynthetic process lipid A biosynthetic process carbohydrate derivative metabolic process lipid biosynthetic process phospholipid metabolic process phosphate-containing compound metabolic process lipooligosaccharide biosynthetic process phosphorus metabolic process carbohydrate derivative biosynthetic process membrane lipid metabolic process lipooligosaccharide metabolic process cellular metabolic process liposaccharide metabolic process primary metabolic process glycolipid biosynthetic process phospholipid biosynthetic process lipid A metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process cellular lipid metabolic process metabolic process cellular process membrane lipid biosynthetic process lipid metabolic process response to stimulus response to chemical response to antibiotic lipopolysaccharide biosynthetic process carbohydrate metabolic process polysaccharide biosynthetic process carbohydrate biosynthetic process macromolecule biosynthetic process lipopolysaccharide metabolic process polysaccharide metabolic process macromolecule metabolic process nucleoside phosphate metabolic process nucleotide-sugar metabolic process UDP-D-xylose metabolic process nucleobase-containing compound biosynthetic process nucleobase-containing compound metabolic process nucleobase-containing small molecule metabolic process nucleoside phosphate biosynthetic process small molecule metabolic process UDP-D-xylose biosynthetic process nucleotide-sugar biosynthetic process UDP-4-deoxy-4-formamido-beta-L-arabinopyranose metabolic process amino sugar biosynthetic process UDP-4-deoxy-4-formamido-beta-L-arabinopyranose biosynthetic process amino sugar metabolic process	protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR050177	Bifunctional lipid A modification and metabolic enzymes	Family
A	IPR045869	Bifunctional polymyxin resistance protein ArnA-like, extended (e) SDRs	Domain
A	IPR036477	Formyl transferase, N-terminal domain superfamily	Homologous Superfamily
A	IPR021168	Bifunctional polymyxin resistance protein, ArnA	Family
A	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A	IPR001509	NAD-dependent epimerase/dehydratase	Domain
A	IPR002376	Formyl transferase, N-terminal	Domain
A	IPR005793	Formyl transferase, C-terminal	Domain
A	IPR011034	Formyl transferase-like, C-terminal domain superfamily	Homologous Superfamily

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.