Annotations: 1Q15

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1q15a1	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	N-type ATP pyrophosphatases	beta-Lactam synthetase	(Pectobacterium carotovorum ) [TaxId: 554 ],	SCOPe (2.08)
A	d1q15a2	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Class II glutamine amidotransferases	beta-Lactam synthetase	(Pectobacterium carotovorum ) [TaxId: 554 ],	SCOPe (2.08)
B [auth C]	d1q15c1	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	N-type ATP pyrophosphatases	beta-Lactam synthetase	(Pectobacterium carotovorum ) [TaxId: 554 ],	SCOPe (2.08)
B [auth C]	d1q15c2	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Class II glutamine amidotransferases	beta-Lactam synthetase	(Pectobacterium carotovorum ) [TaxId: 554 ],	SCOPe (2.08)
C [auth B]	d1q15b1	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	N-type ATP pyrophosphatases	beta-Lactam synthetase	(Pectobacterium carotovorum ) [TaxId: 554 ],	SCOPe (2.08)
C [auth B]	d1q15b2	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Class II glutamine amidotransferases	beta-Lactam synthetase	(Pectobacterium carotovorum ) [TaxId: 554 ],	SCOPe (2.08)
D	d1q15d1	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	N-type ATP pyrophosphatases	beta-Lactam synthetase	(Pectobacterium carotovorum ) [TaxId: 554 ],	SCOPe (2.08)
D	d1q15d2	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Class II glutamine amidotransferases	beta-Lactam synthetase	(Pectobacterium carotovorum ) [TaxId: 554 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Class II glutamine amidotransferases	8039529	3000131	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8039528	3001593	SCOP2B (2022-06-29)
B [auth C]	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8039528	3001593	SCOP2B (2022-06-29)
B [auth C]	SCOP2B Superfamily	Class II glutamine amidotransferases	8039529	3000131	SCOP2B (2022-06-29)
C [auth B]	SCOP2B Superfamily	Class II glutamine amidotransferases	8039529	3000131	SCOP2B (2022-06-29)
C [auth B]	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8039528	3001593	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Adenine nucleotide alpha hydrolases-like	8039528	3001593	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Class II glutamine amidotransferases	8039529	3000131	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	PF09147	e1q15A1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Class II glutamine amidotransferases	F: PF09147	ECOD (1.6)
A	PF00733	e1q15A2	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: PF00733	ECOD (1.6)
B [auth C]	PF09147	e1q15C1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Class II glutamine amidotransferases	F: PF09147	ECOD (1.6)
B [auth C]	PF00733	e1q15C2	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: PF00733	ECOD (1.6)
C [auth B]	PF09147	e1q15B1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Class II glutamine amidotransferases	F: PF09147	ECOD (1.6)
C [auth B]	PF00733	e1q15B2	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: PF00733	ECOD (1.6)
D	PF09147	e1q15D1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Class II glutamine amidotransferases	F: PF09147	ECOD (1.6)
D	PF00733	e1q15D2	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: PF00733	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
A	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
B [auth C]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
B [auth C]	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
C [auth B]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
C [auth B]	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
D	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
D	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B [auth C], C [auth B], D	PF00733	Asparagine synthase (Asn_synthase)	Asparagine synthase	This family is always found associated with Pfam:PF00310. Members of this family catalyse the conversion of aspartate to asparagine.	Domain
A, B [auth C], C [auth B], D	PF09147	Carbapenam-3-carboxylate synthase, N-terminal (CarA_N)	Carbapenam-3-carboxylate synthase, N-terminal	This domain is found in the N-terminal of carbapenam-3-carboxylate synthase (carA), and is composed of two antiparallel six-stranded beta-sheets that form a sandwich, flanked on each side by two alpha-helices [1]. carA is involved in the biosynthesis ...	This domain is found in the N-terminal of carbapenam-3-carboxylate synthase (carA), and is composed of two antiparallel six-stranded beta-sheets that form a sandwich, flanked on each side by two alpha-helices [1]. carA is involved in the biosynthesis of carbapenam-3-carboxylate, a beta-lactam antibiotic of the carbapenem class. It catalyses the ATP-dependent formation of (3S,5S)-carbapenam-3-carboxylate from (2S,5S)-5-carboxymethylproline [2,3,4].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B [auth C], C [auth B], D	CarA	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 carbon-nitrogen ligase activity, with glutamine as amido-N-donor asparagine synthase (glutamine-hydrolyzing) activity catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity	oxoacid metabolic process cellular biosynthetic process aspartate family amino acid biosynthetic process asparagine biosynthetic process aspartate family amino acid metabolic process organonitrogen compound biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process oxoacid metabolic process cellular biosynthetic process aspartate family amino acid biosynthetic process asparagine biosynthetic process aspartate family amino acid metabolic process organonitrogen compound biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process organonitrogen compound metabolic process small molecule biosynthetic process cellular metabolic process carboxylic acid metabolic process primary metabolic process L-amino acid biosynthetic process L-amino acid metabolic process proteinogenic amino acid metabolic process asparagine metabolic process amino acid biosynthetic process biosynthetic process proteinogenic amino acid biosynthetic process metabolic process cellular process alpha-amino acid biosynthetic process antibiotic metabolic process antibiotic biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B [auth C], C [auth B], D	IPR015230	Carbapenam-3-carboxylate synthase, N-terminal	Domain
A, B [auth C], C [auth B], D	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
A, B [auth C], C [auth B], D	IPR001962	Asparagine synthase	Domain
A, B [auth C], C [auth B], D	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold	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.