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InterPro: IPR000873 AMP-dependent synthetase/ligase

Protein matches Help

UniProtKB

Matches:

25950 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR000873 AMP-dep_Synth/Lig

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00501	AMP-binding	25950
Signatures in BioMart

InterPro Relationships Help

Children

IPR010071 Amino acid adenylation

Found in

IPR005914 Acetoacetyl-CoA synthase
IPR010192 O-succinylbenzoate-CoA ligase
IPR011880 Phenylacetate-CoA ligase
IPR011904 Acetate--CoA ligase
IPR011957 Benzoate-CoA ligase family
IPR011963 2,3-dihydroxybenzoate-AMP ligase
IPR012694 Propionate--CoA ligase
IPR012743 4-coumarate--CoA ligase
IPR017523 Conserved hypothetical protein CHP03089
IPR017529 Acyl-CoA ligase (AMP-forming), exosortase system type 1 associated
IPR017618 Dicarboxylate-CoA ligase PimA
IPR017621 Cyclohexanecarboxylate-CoA ligase
IPR017720 Coenzyme F390 synthetase

Contains

IPR020459 AMP-binding
IPR020845 AMP-binding, conserved site

GO Term annotation Help

Process

GO:0008152 metabolic process

Function

GO:0003824 catalytic activity

InterPro annotation

Entry Details in BioMart

Abstract

A number of prokaryotic and eukaryotic enzymes, which appear to act via an ATP-dependent covalent binding of AMP to their substrate, share a region of sequence similarity [1, 2, 3]. This region is a Ser/Thr/Gly-rich domain that is further characterised by a conserved Pro-Lys-Gly triplet. The family of enzymes includes luciferase, long chain fatty acid Co-A ligase, acetyl-CoA synthetase and various other closely-related synthetases.

Structural links Help

PDB - click here

SCOP: e.23.1.1

CATH: 2.30.38.10 , 3.30.300.30 , 3.40.50.980

Database links Help

PDBe-motif: PS00455

PROSITE doc: PDOC00427

PANDIT: PF00501

Blocks: IPB000873

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000873

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O35488 Very long-chain acyl-CoA synthetase

Q01574 Acetyl-coenzyme A synthetase 1

Q08AH3 Acyl-coenzyme A synthetase ACSM2A, mitochondrial

Q21166 Acetoacetyl-CoA synthetase

Q9V3S9 Very long-chain-fatty-acid--CoA ligase bubblegum

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR011904	Acetate--CoA ligase
IPR020845	AMP-binding, conserved site
IPR005914	Acetoacetyl-CoA synthase
IPR000873	AMP-dependent synthetase/ligase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain

Publications Open in usermanual
1.	Smith DJ, Earl AJ, Turner G. The multifunctional peptide synthetase performing the first step of penicillin biosynthesis in Penicillium chrysogenum is a 421,073 dalton protein similar to Bacillus brevis peptide antibiotic synthetases. EMBO J. 9 2743-50 1990 [PubMed: 2118102] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=2118102&action=stream&blobtype=pdf
2.	Schroder J. Protein sequence homology between plant 4-coumarate:CoA ligase and firefly luciferase. Nucleic Acids Res. 17 460 1989 [PubMed: 2911486] http://dx.doi.org/10.1093/nar/17.1.460
3.	Mallonee DH, White WB, Hylemon PB. Cloning and sequencing of a bile acid-inducible operon from Eubacterium sp. strain VPI 12708. J. Bacteriol. 172 7011-9 1990 [PubMed: 2254270] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=2254270&action=stream&blobtype=pdf

Additional Reading Open in usermanual
	Jogl G, Tong L. Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP. Biochemistry 43 2004 1425-31 [PubMed: 14769018] http://dx.doi.org/10.1021/bi035911a
	Conti E, Franks NP, Brick P. Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure 4 1996 287-98 [PubMed: 8805533] http://dx.doi.org/10.1016/S0969-2126(96)00033-0
	Hisanaga Y, Ago H, Nakagawa N, Hamada K, Ida K, Yamamoto M, Hori T, Arii Y, Sugahara M, Kuramitsu S, Yokoyama S, Miyano M. Structural basis of the substrate-specific two-step catalysis of long chain fatty acyl-CoA synthetase dimer. J. Biol. Chem. 279 2004 31717-26 [PubMed: 15145952] http://dx.doi.org/10.1074/jbc.M400100200
	Wu R, Reger AS, Cao J, Gulick AM, Dunaway-Mariano D. Rational redesign of the 4-chlorobenzoate binding site of 4-chlorobenzoate: coenzyme a ligase for expanded substrate range. Biochemistry 46 2007 14487-99 [PubMed: 18027984] http://dx.doi.org/10.1021/bi701609w
	Reger AS, Wu R, Dunaway-Mariano D, Gulick AM. Structural characterization of a 140 degrees domain movement in the two-step reaction catalyzed by 4-chlorobenzoate:CoA ligase. Biochemistry 47 2008 8016-25 [PubMed: 18620418] http://dx.doi.org/10.1021/bi800696y
	Gulick AM, Lu X, Dunaway-Mariano D. Crystal structure of 4-chlorobenzoate:CoA ligase/synthetase in the unliganded and aryl substrate-bound states. Biochemistry 43 2004 8670-9 [PubMed: 15236575] http://dx.doi.org/10.1021/bi049384m

InterPro 23.1