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InterPro: IPR013817 Pre-ATP-grasp fold
Protein matches
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UniProtKB Matches: 13920 proteins |
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Accession
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IPR013817 Pre-ATP_grasp |
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Type
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Domain |
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Signatures
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InterPro Relationships
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Parent
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IPR016185 PreATP-grasp-like fold
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Children
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IPR005481 Carbamoyl phosphate synthase, large subunit, N-terminal
IPR020562 Phosphoribosylglycinamide synthetase, N-domain
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Found in
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IPR000115 Phosphoribosylglycinamide synthetase
IPR004215 Prokaryotic glutathione synthetase, N-terminal
IPR005862 Phosphoribosylglycinamide formyltransferase 2
IPR005875 Phosphoribosylaminoimidazole carboxylase, ATPase subunit
IPR005905 D-alanine--D-alanine ligase
IPR006284 Glutathione synthetase, prokaryotic
IPR011127 D-alanine--D-alanine ligase, N-terminal
IPR016301 Phosphoribosylaminoimidazole carboxylase
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Contains
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IPR000291 D-alanine--D-alanine ligase/VANA/B/C, conserved site
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GO Term annotation
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Function
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GO:0003824 catalytic activity
GO:0005524 ATP binding
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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The ATP-grasp fold is one of several distinct ATP-binding folds, and is found in enzymes that catalyze the formation of amide bonds, catalyzing the ATP-dependent ligation of a carboxylate-containing molecule to an amino or thiol group-containing molecule [1]. This fold is found in many different enzyme families, including various peptide synthetases, biotin carboxylase, synapsin, succinyl-CoA synthetase, pyruvate phosphate dikinase, and glutathione synthetase, amongst others [2]. These enzymes contribute predominantly to macromolecular synthesis, using ATP-hydrolysis to activate their substrates.
This entry represents the pre-ATP-grasp domain, which precedes the ATP-grasp domain in all superfamily members, and which usually occurs at the N terminus of the protein. The structure of the pre-ATP-grasp domain consists of alpha/beta/alpha in three layers, and is possibly a rudiment form of the Rossmann-fold. This domain can have a substrate-binding function.
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Structural links
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Database links
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Example proteins
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O00763 Acetyl-CoA carboxylase 2
O17732 Pyruvate carboxylase 1
P00967 Trifunctional purine biosynthetic protein adenosine-3
Q00955 Acetyl-CoA carboxylase
Q05920 Pyruvate carboxylase, mitochondrial
More proteins
Example Proteins Key
| InterPro entry accession number/name and structure databases |
Colour code |
| IPR013785 |
Aldolase-type TIM barrel |
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| IPR002376 |
Formyl transferase, N-terminal |
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| IPR005479 |
Carbamoyl phosphate synthetase, large subunit, ATP-binding |
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| IPR011764 |
Biotin carboxylation domain |
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| IPR000022 |
Carboxyl transferase |
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| IPR011761 |
ATP-grasp fold |
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| IPR011762 |
Acetyl-coenzyme A carboxyltransferase, N-terminal |
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| IPR011763 |
Acetyl-coenzyme A carboxyltransferase, C-terminal |
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| IPR001555 |
Phosphoribosylglycinamide formyltransferase, active site |
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| IPR011053 |
Single hybrid motif |
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| IPR010918 |
AIR synthase related protein, C-terminal |
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| IPR004733 |
Phosphoribosylformylglycinamidine cyclo-ligase |
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| IPR011054 |
Rudiment single hybrid motif |
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| IPR020561 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain |
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| IPR020560 |
Phosphoribosylglycinamide synthetase, C-domain |
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| IPR000089 |
Biotin/lipoyl attachment |
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| IPR020562 |
Phosphoribosylglycinamide synthetase, N-domain |
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| IPR000891 |
Pyruvate carboxyltransferase |
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| IPR000115 |
Phosphoribosylglycinamide synthetase |
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| IPR005481 |
Carbamoyl phosphate synthase, large subunit, N-terminal |
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| IPR013815 |
ATP-grasp fold, subdomain 1 |
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| IPR013816 |
ATP-grasp fold, subdomain 2 |
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| IPR013817 |
Pre-ATP-grasp fold |
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| IPR001882 |
Biotin-binding site |
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| IPR020559 |
Phosphoribosylglycinamide synthetase, conserved site |
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| IPR004607 |
Phosphoribosylglycinamide formyltransferase |
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| IPR005482 |
Biotin carboxylase, C-terminal |
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| IPR016188 |
PurM, N-terminal-like |
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| IPR013537 |
Acetyl-CoA carboxylase, central region |
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| IPR003379 |
Carboxylase, conserved domain |
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| IPR016185 |
PreATP-grasp-like fold |
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| IPR005930 |
Pyruvate carboxylase |
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| IPR000728 |
AIR synthase related protein |
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ModBase |
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SWISS-MODEL |
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PDB Chain |
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CATH Domain |
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SCOP Domain |
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Additional Reading
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Thoden JB, Holden HM, Firestine SM.
Structural analysis of the active site geometry of N5-carboxyaminoimidazole ribonucleotide synthetase from Escherichia coli.
Biochemistry 47 2008 13346-53
[PubMed: 19053251]
http://dx.doi.org/10.1021/bi801734z
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Mochalkin I, Miller JR, Evdokimov A, Lightle S, Yan C, Stover CK, Waldrop GL.
Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase.
Protein Sci. 17 2008 1706-18
[PubMed: 18725455]
http://dx.doi.org/10.1110/ps.035584.108
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Shen Y, Chou CY, Chang GG, Tong L.
Is dimerization required for the catalytic activity of bacterial biotin carboxylase?
Mol. Cell 22 2006 807-18
[PubMed: 16793549]
http://dx.doi.org/10.1016/j.molcel.2006.04.026
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Lee JH, Na Y, Song HE, Kim D, Park BH, Rho SH, Im YJ, Kim MK, Kang GB, Lee DS, Eom SH.
Crystal structure of the apo form of D-alanine: D-alanine ligase (Ddl) from Thermus caldophilus: a basis for the substrate-induced conformational changes.
Proteins 64 2006 1078-82
[PubMed: 16779845]
http://dx.doi.org/10.1002/prot.20927
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Kondo S, Nakajima Y, Sugio S, Sueda S, Islam MN, Kondo H.
Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans.
Acta Crystallogr. D Biol. Crystallogr. 63 2007 885-90
[PubMed: 17642515]
http://dx.doi.org/10.1107/S0907444907029423
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InterPro 23.1
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