SCOP 1.71: Domain d1hm9a1: 1hm9 A:252-459

Lineage for d1hm9a1 (1hm9 A:252-459)

1. Root: SCOP 1.71

2. Class b: All beta proteins [48724] (149 folds)

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

4. Superfamily b.81.1: Trimeric LpxA-like enzymes [51161] (6 families)
   superhelical turns are made of three short strands; duplication: the sequence hexapeptide repeats correspond to individual strands

5. Family b.81.1.4: N-acetylglucosamine 1-phosphate uridyltransferase GlmU, C-terminal domain [51171] (1 protein)
   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] (2 species)

7. Species Streptococcus pneumoniae [TaxId:1313] [63852] (5 PDB entries)

8. Domain d1hm9a1: 1hm9 A:252-459 [65866]
   Other proteins in same PDB: d1hm9a2, d1hm9b2

Details for d1hm9a1

PDB Entry: 1hm9, 1.75 Å

PDB Description: crystal structure of s.pneumoniae n-acetylglucosamine-1-phosphate uridyltransferase, glmu, bound to acetyl coenzyme a and udp-n- acetylglucosamine

SCOP Domain Sequences for d1hm9a1:

Sequence; same for both SEQRES and ATOM records:

>d1hm9a1 b.81.1.4 (A:252-459) N-acetylglucosamine 1-phosphate uridyltransferase GlmU, C-terminal domain {Streptococcus pneumoniae}
vsfvnpeatyididveiapevqieanvilkgqtkigaetvltngtyvvdstigagavitn
smieessvadgvtvgpyahirpnsslgaqvhignfvevkgssigentkaghltyigncev
gsnvnfgagtitvnydgknkyktvigdnvfvgsnstiiapvelgdnslvgagstitkdvp
adaiaigrgrqinkdeyatrlphhpknq

Timeline for d1hm9a1:

• d1hm9a1 first appeared in SCOP 1.59
  
• d1hm9a1 appears in SCOP 1.69
  
• d1hm9a1 appears in SCOP 1.73
  
• d1hm9a1 appears in the current release, SCOPe 2.08