SCOPe 2.08: Domain d2gpwb3: 2gpw B:115-330

Lineage for d2gpwb3 (2gpw B:115-330)

1. Root: SCOPe 2.08

2. Class d: Alpha and beta proteins (a+b) [53931] (396 folds)

3. Fold d.142: ATP-grasp [56058] (2 superfamilies)
   Consists of two subdomains with different alpha+beta folds
   shares functional and structural similarities with the PIPK and protein kinase superfamilies

4. Superfamily d.142.1: Glutathione synthetase ATP-binding domain-like [56059] (11 families)

5. Family d.142.1.2: BC ATP-binding domain-like [56067] (7 proteins)

6. Protein Biotin carboxylase (BC), domain 2 [56068] (2 species)
   subunit of acetyl-CoA and pyruvate carboxylases

7. Species Escherichia coli [TaxId:562] [56069] (24 PDB entries)

8. Domain d2gpwb3: 2gpw B:115-330 [135502]
   Other proteins in same PDB: d2gpwa1, d2gpwa2, d2gpwa4, d2gpwb1, d2gpwb2, d2gpwb4, d2gpwc1, d2gpwc2, d2gpwc4, d2gpwd1, d2gpwd2, d2gpwd4
   automated match to d1dv2a3
   mutant

Details for d2gpwb3

PDB Entry: 2gpw, 2.2 Å

PDB Description: crystal structure of the biotin carboxylase subunit, f363a mutant, of acetyl-coa carboxylase from escherichia coli.

PDB Compounds: (B:) biotin carboxylase

SCOPe Domain Sequences for d2gpwb3:

Sequence, based on SEQRES records:

>d2gpwb3 d.142.1.2 (B:115-330) Biotin carboxylase (BC), domain 2 {Escherichia coli [TaxId: 562]}
dkvsaiaamkkagvpcvpgsdgplgddmdknraiakrigypviikasgggggrgmrvvrg
daelaqsismtraeakaafsndmvymekylenprhveiqvladgqgnaiylaerdcsmqr
rhqkvveeapapgitpelrryigercakacvdigyrgagtfeflfengefyfiemntriq
vehpvtemitgvdlikeqlriaagqplsikqeevhv

Sequence, based on observed residues (ATOM records):

>d2gpwb3 d.142.1.2 (B:115-330) Biotin carboxylase (BC), domain 2 {Escherichia coli [TaxId: 562]}
dkvsaiaamkkagvpcvpgsdgplgddmdknraiakrigypviikasggmrvvrgdaela
qsismtraeakadmvymekylenprhveiqvladgqgnaiylaerdcsmqrrhqkvveea
papgitpelrryigercakacvdigyrgagtfeflfengefyfiemntriqvehpvtemi
tgvdlikeqlriaagqplsikqeevhv

Timeline for d2gpwb3:

• d2gpwb3 first appeared in SCOP 1.73
  
• d2gpwb3 appears in SCOPe 2.07