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InterPro: IPR000089 Biotin/lipoyl attachment

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10088 proteins

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Accession List
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Accession

IPR000089 Biotin_lipoyl

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00364	Biotin_lipoyl	9946
PROSITE profile	PS50968	BIOTINYL_LIPOYL	9305
Signatures in BioMart

InterPro Relationships Help

Found in

IPR005930 Pyruvate carboxylase
IPR006255 Dihydrolipoamide succinyltransferase
IPR006256 Dihydrolipoamide acetyltransferase pyruvate dehydrogenase complex
IPR006257 Dihydrolipoamide acetyltransferase, long form
IPR014084 Urea carboxylase
IPR014276 2-oxoglutarate dehydrogenase, E2 component
IPR015761 Lipoamide Acyltransferase
IPR017695 Selenium-dependent molybdenum hydroxylase system protein, YqeB family

Contains

IPR001882 Biotin-binding site
IPR003016 2-oxo acid dehydrogenase, lipoyl-binding site
IPR011053 Single hybrid motif

InterPro annotation

Entry Details in BioMart

Abstract

The biotin / lipoyl attachment domain has a conserved lysine residue that binds biotin or lipoic acid. Biotin plays a catalytic role in some carboxyl transfer reactions and is covalently attached, via an amide bond, to a lysine residue in enzymes requiring this coenzyme [1]. E2 acyltransferases have an essential cofactor, lipoic acid, which is covalently bound via an amide linkage to a lysine group [2]. The lipoic acid cofactor is found in a variety of proteins that include, H-protein of the glycine cleavage system (GCS), mammalian and yeast pyruvate dehydrogenases and fast migrating protein (FMP) (gene acoC) from Ralstonia eutropha (Alcaligenes eutrophus).

Structural links Help

PDB - click here

SCOP: b.84.1.1

CATH: 2.40.50.100

Database links Help

PROSITE doc: PDOC50968

PANDIT: PF00364

Blocks: IPB000089

COMe: PRX001138

Pfam Clan: CL0105.9

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000089

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O00330 Pyruvate dehydrogenase protein X component, mitochondrial

O17732 Pyruvate carboxylase 1

P53395 Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial

Q00955 Acetyl-CoA carboxylase

Q0WQF7 Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013785	Aldolase-type TIM barrel
IPR004167	E3 binding
IPR003016	2-oxo acid dehydrogenase, lipoyl-binding site
IPR011764	Biotin carboxylation domain
IPR005479	Carbamoyl phosphate synthetase, large subunit, ATP-binding
IPR000022	Carboxyl transferase
IPR011761	ATP-grasp fold
IPR011762	Acetyl-coenzyme A carboxyltransferase, N-terminal
IPR011763	Acetyl-coenzyme A carboxyltransferase, C-terminal
IPR011053	Single hybrid motif
IPR011054	Rudiment single hybrid motif
IPR000089	Biotin/lipoyl attachment
IPR000891	Pyruvate carboxyltransferase
IPR005481	Carbamoyl phosphate synthase, large subunit, N-terminal
IPR013816	ATP-grasp fold, subdomain 2
IPR013817	Pre-ATP-grasp fold
IPR001078	2-oxoacid dehydrogenase acyltransferase, catalytic domain
IPR001882	Biotin-binding site
IPR005482	Biotin carboxylase, C-terminal
IPR013537	Acetyl-CoA carboxylase, central region
IPR003379	Carboxylase, conserved domain
IPR016185	PreATP-grasp-like fold
IPR006257	Dihydrolipoamide acetyltransferase, long form
IPR005930	Pyruvate carboxylase
IPR015761	Lipoamide Acyltransferase
	ModBase
	SWISS-MODEL
	PDB Chain
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Shenoy BC, Xie Y, Park VL, Kumar GK, Beegen H, Wood HG, Samols D. The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis. J. Biol. Chem. 267 18407-12 1992 [PubMed: 1526981] http://intl.jbc.org/cgi/reprint/267/26/18407.pdf
2.	Russell GC, Guest JR. Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme. Biochim. Biophys. Acta 1076 225-32 1991 [PubMed: 1825611] http://dx.doi.org/10.1016/0167-4838(91)90271-Z

Additional Reading Open in usermanual
	Devedjiev Y, Steussy CN, Vassylyev DG. Crystal structure of an asymmetric complex of pyruvate dehydrogenase kinase 3 with lipoyl domain 2 and its biological implications. J. Mol. Biol. 370 2007 407-16 [PubMed: 17532006] http://dx.doi.org/10.1016/j.jmb.2007.04.083
	Kato M, Li J, Chuang JL, Chuang DT. Distinct structural mechanisms for inhibition of pyruvate dehydrogenase kinase isoforms by AZD7545, dichloroacetate, and radicicol. Structure 15 2007 992-1004 [PubMed: 17683942] http://dx.doi.org/10.1016/j.str.2007.07.001
	Reche PA, Howard MJ, Broadhurst RW, Perham RN. Heteronuclear NMR studies of the specificity of the post-translational modification of biotinyl domains by biotinyl protein ligase. FEBS Lett. 479 2000 93-8 [PubMed: 10981714] http://dx.doi.org/10.1016/S0014-5793(00)01829-9
	Perham RN, Reche PA. Swinging arms in multifunctional enzymes and the specificity of post-translational modification. Biochem. Soc. Trans. 26 1998 299-303 [PubMed: 9765868] http://www.biochemsoctrans.org/bst/026/0299/bst0260299.htm
	Athappilly FK, Hendrickson WA. Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing. Structure 3 1995 1407-19 [PubMed: 8747466] http://dx.doi.org/10.1016/S0969-2126(01)00277-5
	Cui G, Nan B, Hu J, Wang Y, Jin C, Xia B. Identification and solution structures of a single domain biotin/lipoyl attachment protein from Bacillus subtilis. J. Biol. Chem. 281 2006 20598-607 [PubMed: 16699181] http://dx.doi.org/10.1074/jbc.M602660200
	Ricaud PM, Howard MJ, Roberts EL, Broadhurst RW, Perham RN. Three-dimensional structure of the lipoyl domain from the dihydrolipoyl succinyltransferase component of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli. J. Mol. Biol. 264 1996 179-90 [PubMed: 8950276] http://dx.doi.org/10.1006/jmbi.1996.0632
	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
	Kato M, Chuang JL, Tso SC, Wynn RM, Chuang DT. Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex. EMBO J. 24 2005 1763-74 [PubMed: 15861126] http://dx.doi.org/10.1038/sj.emboj.7600663

InterPro 23.1