SCOPe 2.07: Domain d1s1ma1: 1s1m A:287-544

Lineage for d1s1ma1 (1s1m A:287-544)

1. Root: SCOPe 2.07

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

3. Fold c.23: Flavodoxin-like [52171] (15 superfamilies)
   3 layers, a/b/a; parallel beta-sheet of 5 strand, order 21345

4. Superfamily c.23.16: Class I glutamine amidotransferase-like [52317] (10 families)
   conserved positions of the oxyanion hole and catalytic nucleophile; different constituent families contain different additional structures

5. Family c.23.16.1: Class I glutamine amidotransferases (GAT) [52318] (12 proteins)
   contains a catalytic Cys-His-Glu triad

6. Protein CTP synthase PyrG, C-terminal domain [110481] (2 species)

7. Species Escherichia coli [TaxId:562] [110482] (1 PDB entry)
   Uniprot P08398

8. Domain d1s1ma1: 1s1m A:287-544 [105201]
   Other proteins in same PDB: d1s1ma2, d1s1mb2
   complexed with iod, mg, mpd, so4

Details for d1s1ma1

PDB Entry: 1s1m, 2.3 Å

PDB Description: Crystal Structure of E. Coli CTP Synthetase

PDB Compounds: (A:) CTP synthase

SCOPe Domain Sequences for d1s1ma1:

Sequence, based on SEQRES records:

>d1s1ma1 c.23.16.1 (A:287-544) CTP synthase PyrG, C-terminal domain {Escherichia coli [TaxId: 562]}
vsevtigmvgkyielpdayksviealkhgglknrvsvniklidsqdvetrgveilkglda
ilvpggfgyrgvegmittarfarennipylgiclgmqvalidyarhvanmenanstefvp
dckypvvalitewrdengnvevrseksdlggtmrlgaqqcqlvddslvrqlynaptiver
hrhryevnnmllkqiedaglrvagrsgddqlveiievpnhpwfvacqfhpeftstprdgh
plfagfvkaasefqkrqa

Sequence, based on observed residues (ATOM records):

>d1s1ma1 c.23.16.1 (A:287-544) CTP synthase PyrG, C-terminal domain {Escherichia coli [TaxId: 562]}
vsevtigmvgkyielpdayksviealkhgglknrvsvniklidsqdvetrgveilkglda
ilvpggfgyrgvegmittarfarennipylgiclgmqvalidyarhvanmenanstefvp
dckypvvalitewrdengnvetmrlgaqqcqlvddslvrqlynaptiverhrhryevnnm
llkqiedaglrvagrsgddqlveiievpnhpwfvacqfhpeftstprdghplfagfvkaa
sefqkrqa

Timeline for d1s1ma1:

• d1s1ma1 first appeared in SCOP 1.69
  
• d1s1ma1 appears in SCOPe 2.06
  
• d1s1ma1 appears in the current release, SCOPe 2.08