Annotations: 1D7A

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1d7aa_	Alpha and beta proteins (a/b)	Flavodoxin-like	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1d7ab_	Alpha and beta proteins (a/b)	Flavodoxin-like	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1d7ac_	Alpha and beta proteins (a/b)	Flavodoxin-like	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d1d7ad_	Alpha and beta proteins (a/b)	Flavodoxin-like	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
E [auth L]	d1d7al_	Alpha and beta proteins (a/b)	Flavodoxin-like	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
F [auth M]	d1d7am_	Alpha and beta proteins (a/b)	Flavodoxin-like	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
G [auth N]	d1d7an_	Alpha and beta proteins (a/b)	Flavodoxin-like	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
H [auth O]	d1d7ao_	Alpha and beta proteins (a/b)	Flavodoxin-like	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	(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	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase PurE)	8044106	3001291	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase PurE)	8044106	3001291	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase PurE)	8044106	3001291	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase PurE)	8044106	3001291	SCOP2B (2022-06-29)
E [auth L]	SCOP2B Superfamily	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase PurE)	8044106	3001291	SCOP2B (2022-06-29)
F [auth M]	SCOP2B Superfamily	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase PurE)	8044106	3001291	SCOP2B (2022-06-29)
G [auth N]	SCOP2B Superfamily	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase PurE)	8044106	3001291	SCOP2B (2022-06-29)
H [auth O]	SCOP2B Superfamily	N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase PurE)	8044106	3001291	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	AIRC	e1d7aA1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	F: AIRC	ECOD (1.6)
B	AIRC	e1d7aB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	F: AIRC	ECOD (1.6)
C	AIRC	e1d7aC1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	F: AIRC	ECOD (1.6)
D	AIRC	e1d7aD1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	F: AIRC	ECOD (1.6)
E [auth L]	AIRC	e1d7aL1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	F: AIRC	ECOD (1.6)
F [auth M]	AIRC	e1d7aM1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	F: AIRC	ECOD (1.6)
G [auth N]	AIRC	e1d7aN1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	F: AIRC	ECOD (1.6)
H [auth O]	AIRC	e1d7aO1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)	F: AIRC	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
B	3.40.50.1970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
C	3.40.50.1970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
D	3.40.50.1970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
E [auth L]	3.40.50.1970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
F [auth M]	3.40.50.1970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
G [auth N]	3.40.50.1970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
H [auth O]	3.40.50.1970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E [auth L], A, B, C, D, E [auth L], F [auth M], G [auth N], H [auth O]	PF00731	AIR carboxylase (AIRC)	AIR carboxylase	Members of this family catalyse the decarboxylation of 1-(5-phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR). This family catalyse the sixth step of de novo purine biosynthesis. Some members of this family contain two copies of this domain.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E [auth L], A, B, C, D, E [auth L], F [auth M], G [auth N], H [auth O]	PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE	isomerase activity 5-(carboxyamino)imidazole ribonucleotide mutase activity catalytic activity intramolecular transferase activity identical protein binding protein binding binding	ribose phosphate metabolic process IMP metabolic process purine ribonucleoside monophosphate biosynthetic process nucleotide biosynthetic process organonitrogen compound biosynthetic process carbohydrate derivative metabolic process purine ribonucleotide biosynthetic process nucleobase-containing compound metabolic process ribonucleotide biosynthetic process purine nucleoside monophosphate biosynthetic process purine ribonucleoside monophosphate metabolic process purine nucleotide metabolic process organic substance metabolic process ribonucleotide metabolic process ribonucleoside monophosphate metabolic process ribose phosphate metabolic process IMP metabolic process purine ribonucleoside monophosphate biosynthetic process nucleotide biosynthetic process organonitrogen compound biosynthetic process carbohydrate derivative metabolic process purine ribonucleotide biosynthetic process nucleobase-containing compound metabolic process ribonucleotide biosynthetic process purine nucleoside monophosphate biosynthetic process purine ribonucleoside monophosphate metabolic process purine nucleotide metabolic process organic substance metabolic process ribonucleotide metabolic process ribonucleoside monophosphate metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process purine nucleoside monophosphate metabolic process phosphate-containing compound metabolic process organic substance biosynthetic process small molecule metabolic process phosphorus metabolic process ribose phosphate biosynthetic process nucleoside monophosphate metabolic process nucleoside phosphate metabolic process carbohydrate derivative biosynthetic process organonitrogen compound metabolic process cellular metabolic process primary metabolic process nucleotide metabolic process nucleobase-containing compound biosynthetic process nucleoside monophosphate biosynthetic process purine-containing compound metabolic process organic cyclic compound metabolic process IMP biosynthetic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process organic cyclic compound biosynthetic process nucleoside phosphate biosynthetic process metabolic process cellular process 'de novo' IMP biosynthetic process purine ribonucleotide metabolic process ribonucleoside monophosphate biosynthetic process purine nucleotide biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E [auth L], A, B, C, D, E [auth L], F [auth M], G [auth N], H [auth O]	IPR033747	Class I PurE	Domain
A, B, C, D, E [auth L], A, B, C, D, E [auth L], F [auth M], G [auth N], H [auth O]	IPR000031	PurE domain	Domain
A, B, C, D, E [auth L], A, B, C, D, E [auth L], F [auth M], G [auth N], H [auth O]	IPR024694	PurE, prokaryotic type	Family

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.