SCOP 1.73: Domain d1piia1: 1pii A:255-452

Lineage for d1piia1 (1pii A:255-452)

1. Root: SCOP 1.73

2. Class c: Alpha and beta proteins (a/b) [51349] (141 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (33 superfamilies)
   contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
   the first seven superfamilies have similar phosphate-binding sites

4. Superfamily c.1.2: Ribulose-phoshate binding barrel [51366] (6 families)

5. Family c.1.2.4: Tryptophan biosynthesis enzymes [51381] (3 proteins)

6. Protein N-(5'phosphoribosyl)antranilate isomerase, PRAI [51382] (3 species)

7. Species Escherichia coli [TaxId:562] [51383] (1 PDB entry)
   merged in bifunctional enzyme with IPG synthase

8. Domain d1piia1: 1pii A:255-452 [28559]
   Other proteins in same PDB: d1piia2
   complexed with po4

Details for d1piia1

PDB Entry: 1pii, 2 Å

PDB Description: three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from escherichia coli refined at 2.0 angstroms resolution

PDB Compounds: (A:) n-(5'phosphoribosyl)anthranilate isomerase

SCOP Domain Sequences for d1piia1:

Sequence; same for both SEQRES and ATOM records:

>d1piia1 c.1.2.4 (A:255-452) N-(5'phosphoribosyl)antranilate isomerase, PRAI {Escherichia coli [TaxId: 562]}
genkvcgltrgqdakaaydagaiygglifvatsprcvnveqaqevmaaaplqyvgvfrnh
diadvvdkakvlslaavqlhgneeqlyidtlrealpahvaiwkalsvgetlparefqhvd
kyvldngqggsgqrfdwsllngqslgnvllagglgadncveaaqtgcagldfnsavesqp
gikdarllasvfqtlray

Timeline for d1piia1:

• d1piia1 first appeared (with stable ids) in SCOP 1.55, called d1pii_2
  
• d1piia1 was called d1pii_2 in SCOP 1.71
  
• d1piia1 appears in SCOP 1.75
  
• d1piia1 appears in the current release, SCOPe 2.08