SCOP 1.71: Domain d1hv9a2: 1hv9 A:4-251

Lineage for d1hv9a2 (1hv9 A:4-251)

1. Root: SCOP 1.71

2. Class c: Alpha and beta proteins (a/b) [51349] (134 folds)

3. Fold c.68: Nucleotide-diphospho-sugar transferases [53447] (1 superfamily)
   3 layers: a/b/a; mixed beta-sheet of 7 strands, order 3214657; strand 6 is antiparallel to the rest

4. Superfamily c.68.1: Nucleotide-diphospho-sugar transferases [53448] (14 families)

5. Family c.68.1.5: UDP-glucose pyrophosphorylase [53461] (2 proteins)

6. Protein N-acetylglucosamine 1-phosphate uridyltransferase GlmU, N-terminal domain [53462] (2 species)

7. Species Escherichia coli [TaxId:562] [53463] (3 PDB entries)

8. Domain d1hv9a2: 1hv9 A:4-251 [34518]
   Other proteins in same PDB: d1hv9a1, d1hv9b1

Details for d1hv9a2

PDB Entry: 1hv9, 2.1 Å

PDB Description: structure of e. coli glmu: analysis of pyrophosphorylase and acetyltransferase active sites

SCOP Domain Sequences for d1hv9a2:

Sequence; same for both SEQRES and ATOM records:

>d1hv9a2 c.68.1.5 (A:4-251) N-acetylglucosamine 1-phosphate uridyltransferase GlmU, N-terminal domain {Escherichia coli}
namsvvilaagkgtrmysdlpkvlhtlagkamvqhvidaanelgaahvhlvyghggdllk
qalkddnlnwvlqaeqlgtghamqqaapffaddedilmlygdvplisvetlqrlrdakpq
ggiglltvklddptgygritrengkvtgivehkdatdeqrqiqeintgiliangadmkrw
lakltnnnaqgeyyitdiialayqegreivavhpqrlsevegvnnrlqlsrlervyqseq
aeklllag

Timeline for d1hv9a2:

• d1hv9a2 first appeared (with stable ids) in SCOP 1.55
  
• d1hv9a2 appears in SCOP 1.69
  
• d1hv9a2 appears in SCOP 1.73
  
• d1hv9a2 appears in the current release, SCOPe 2.08