SCOPe 2.06: Domain d1hv9a2: 1hv9 A:4-251

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

1. Root: SCOPe 2.06

2. Class c: Alpha and beta proteins (a/b) [51349] (148 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] (20 families)

5. Family c.68.1.5: UDP-glucose pyrophosphorylase [53461] (4 proteins)

6. Protein N-acetylglucosamine 1-phosphate uridyltransferase GlmU, N-terminal domain [53462] (3 species)

7. Species Escherichia coli [TaxId:562] [53463] (6 PDB entries)

8. Domain d1hv9a2: 1hv9 A:4-251 [34518]
   Other proteins in same PDB: d1hv9a1, d1hv9b1
   complexed with co, coa, ud1

Details for d1hv9a2

PDB Entry: 1hv9, 2.1 Å

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

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

SCOPe 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 [TaxId: 562]}
namsvvilaagkgtrmysdlpkvlhtlagkamvqhvidaanelgaahvhlvyghggdllk
qalkddnlnwvlqaeqlgtghamqqaapffaddedilmlygdvplisvetlqrlrdakpq
ggiglltvklddptgygritrengkvtgivehkdatdeqrqiqeintgiliangadmkrw
lakltnnnaqgeyyitdiialayqegreivavhpqrlsevegvnnrlqlsrlervyqseq
aeklllag

Timeline for d1hv9a2:

• d1hv9a2 first appeared (with stable ids) in SCOP 1.55
  
• d1hv9a2 appears in SCOPe 2.05
  
• d1hv9a2 appears in SCOPe 2.07
  
• d1hv9a2 appears in the current release, SCOPe 2.08