SCOPe 2.08: Domain d1fwya1: 1fwy A:252-328

Lineage for d1fwya1 (1fwy A:252-328)

1. Root: SCOPe 2.08

2. Class b: All beta proteins [48724] (180 folds)

3. Fold b.81: Single-stranded left-handed beta-helix [51160] (4 superfamilies)
   superhelix turns are made of parallel beta-strands and (short) turns

4. Superfamily b.81.1: Trimeric LpxA-like enzymes [51161] (9 families)
   superhelical turns are made of three short strands; duplication: the sequence hexapeptide repeats correspond to individual strands

5. Family b.81.1.4: GlmU C-terminal domain-like [51171] (4 proteins)
   this is a repeat family; one repeat unit is 2oi5 A:321-339 found in domain

6. Protein N-acetylglucosamine 1-phosphate uridyltransferase GlmU, C-terminal domain [51172] (3 species)

7. Species Escherichia coli [TaxId:562] [51173] (6 PDB entries)

8. Domain d1fwya1: 1fwy A:252-328 [28064]
   Other proteins in same PDB: d1fwya2, d1fwyb2
   truncated form after R331
   complexed with edo, so4, ud1

Details for d1fwya1

PDB Entry: 1fwy, 2.3 Å

PDB Description: crystal structure of n-acetylglucosamine 1-phosphate uridyltransferase bound to udp-glcnac

PDB Compounds: (A:) udp-n-acetylglucosamine pyrophosphorylase

SCOPe Domain Sequences for d1fwya1:

Sequence; same for both SEQRES and ATOM records:

>d1fwya1 b.81.1.4 (A:252-328) N-acetylglucosamine 1-phosphate uridyltransferase GlmU, C-terminal domain {Escherichia coli [TaxId: 562]}
vmlrdparfdlrgtlthgrdveidtnviiegnvtlghrvkigtgcviknsvigddceisp
ytvvedanlaaactigp

Timeline for d1fwya1:

• d1fwya1 first appeared (with stable ids) in SCOP 1.55
  
• d1fwya1 appears in SCOPe 2.07