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InterPro: IPR004143 Biotin/lipoate A/B protein ligase

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4928 proteins

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

Accession

IPR004143 BPL_LipA_LipB

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF03099	BPL_LipA_LipB	4928
Signatures in BioMart

InterPro Relationships Help

Children

IPR000544 Octanoyltransferase

Found in

IPR004408 Biotin--acetyl-CoA-carboxylase ligase

Contains

IPR020605 Octanoyltransferase, conserved site

GO Term annotation Help

Process

GO:0006464 protein modification process

Function

GO:0003824 catalytic activity

InterPro annotation

Entry Details in BioMart

Abstract

This domain is found in biotin protein ligase, lipoate-protein ligase A and B. Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Each organism probably has only one BPL. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine [1]. Lipoate-protein ligase A (LPLA) (octanoyltransferase) catalyses the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes [2].

Structural links Help

PDB - click here

SCOP: d.104.1.2 , d.104.1.3

CATH: 3.30.930.10 , 3.90.1550.10

Database links Help

Enzyme: EC:2.3.1.181

PANDIT: PF03099

Pfam Clan: CL0040.13

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004143

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A6NK58 Putative octanoyltransferase, mitochondrial

A6ZPT1 Putative lipoate-protein ligase A

P0C7R2 Putative lipoyltransferase-like protein, chloroplastic

Q8VCM4 Lipoyltransferase 1, mitochondrial

Q9VN27 Putative octanoyltransferase, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR000544	Octanoyltransferase
IPR004562	Lipoyltransferase/lipoate-protein ligase
IPR020605	Octanoyltransferase, conserved site
IPR004143	Biotin/lipoate A/B protein ligase
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Chapman-Smith A, Cronan JE Jr. The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity. Trends Biochem. Sci. 24 359-63 1999 [PubMed: 10470036] http://dx.doi.org/10.1016/S0968-0004(99)01438-3
2.	Morris TW, Reed KE, Cronan JE Jr. Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product. J. Biol. Chem. 269 16091-100 1994 [PubMed: 8206909] http://intl.jbc.org/cgi/content/abstract/269/23/16091

Additional Reading Open in usermanual
	Wood ZA, Weaver LH, Brown PH, Beckett D, Matthews BW. Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution. J. Mol. Biol. 357 2006 509-23 [PubMed: 16438984] http://dx.doi.org/10.1016/j.jmb.2005.12.066
	Wilson KP, Shewchuk LM, Brennan RG, Otsuka AJ, Matthews BW. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc. Natl. Acad. Sci. U.S.A. 89 1992 9257-61 [PubMed: 1409631] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=1409631&action=stream&blobtype=pdf
	Ma Q, Zhao X, Nasser Eddine A, Geerlof A, Li X, Cronan JE, Kaufmann SH, Wilmanns M. The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine dyad acyltransferase. Proc. Natl. Acad. Sci. U.S.A. 103 2006 8662-7 [PubMed: 16735476] http://dx.doi.org/10.1073/pnas.0510436103
	Reche PA. Lipoylating and biotinylating enzymes contain a homologous catalytic module. Protein Sci. 9 2000 1922-9 [PubMed: 11106165] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=11106165
	McManus E, Luisi BF, Perham RN. Structure of a putative lipoate protein ligase from Thermoplasma acidophilum and the mechanism of target selection for post-translational modification. J. Mol. Biol. 356 2006 625-37 [PubMed: 16384580] http://dx.doi.org/10.1016/j.jmb.2005.11.057
	Bagautdinov B, Kuroishi C, Sugahara M, Kunishima N. Crystal structures of biotin protein ligase from Pyrococcus horikoshii OT3 and its complexes: structural basis of biotin activation. J. Mol. Biol. 353 2005 322-33 [PubMed: 16169557] http://dx.doi.org/10.1016/j.jmb.2005.08.032
	Bagautdinov B, Matsuura Y, Bagautdinova S, Kunishima N. Protein biotinylation visualized by a complex structure of biotin protein ligase with a substrate. J. Biol. Chem. 283 2008 14739-50 [PubMed: 18372281] http://dx.doi.org/10.1074/jbc.M709116200

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