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InterPro: IPR003142 Biotin protein ligase, C-terminal

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1284 proteins

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Accession

IPR003142 BPL_C

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02237	BPL_C	1284
Signatures in BioMart

InterPro Relationships Help

Parent

IPR008988 Transcriptional repressor, C-terminal

Found in

IPR004408 Biotin--acetyl-CoA-carboxylase ligase

GO Term annotation Help

Process

GO:0006464 protein modification process

InterPro annotation

Entry Details in BioMart

Abstract

This C-terminal domain has an SH3-like barrel fold, the function of which is unknown. It is found associated with prokaryotic bifunctional transcriptional repressors [1] and eukaryotic enzymes involved in biotin utilization [2, 3].

In Escherichia coli the biotin operon repressor (BirA) is a bifunctional protein. BirA acts both as the acetyl-coA carboxylase biotin holoenzyme synthetase (EC:6.3.4.15) and as the biotin operon repressor. DNA sequence analysis of mutations indicates that the helix-turn-helix DNA binding region is located at the N terminus while mutations affecting enzyme function, although mapping over a large region, are found mainly in the central part of the protein's primary sequence [1].

Structural links Help

PDB - click here

SCOP: b.34.1.1

CATH: 2.30.30.100

Database links Help

Enzyme: EC:6.3.4.15

PANDIT: PF02237

Blocks: IPB003142

Pfam Clan: CL0206.7

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR003142

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P06709 Bifunctional protein birA

P48445 Biotin--protein ligase

P50747 Biotin--protein ligase

Q59014 Putative biotin ligase

Q920N2 Biotin--protein ligase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR011991	Winged helix repressor DNA-binding
IPR004409	Biotin operon repressor, helix-turn-helix region
IPR004408	Biotin--acetyl-CoA-carboxylase ligase
IPR004143	Biotin/lipoate A/B protein ligase
IPR013196	Helix-turn-helix, type 11
IPR003142	Biotin protein ligase, C-terminal
IPR019197	Biotin-protein ligase, N-terminal
IPR008988	Transcriptional repressor, C-terminal
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Brennan RG, Vasu S, Matthews BW, Otsuka AJ. Crystallization of the bifunctional biotin operon repressor. J. Biol. Chem. 264 5 1989 [PubMed: 2642476] http://intl.jbc.org/cgi/reprint/264/1/5.pdf
2.	Suzuki Y, Aoki Y, Ishida Y, Chiba Y, Iwamatsu A, Kishino T, Niikawa N, Matsubara Y, Narisawa K. Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA. Nat. Genet. 8 122-8 1994 [PubMed: 7842009] http://dx.doi.org/10.1038/ng1094-122
3.	Tissot G, Douce R, Alban C. Evidence for multiple forms of biotin holocarboxylase synthetase in pea (Pisum sativum) and in Arabidopsis thaliana: subcellular fractionation studies and isolation of a cDNA clone. Biochem. J. 323 ( Pt 1) 179-88 1997 [PubMed: 9173880] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=9173880

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
	Weaver LH, Kwon K, Beckett D, Matthews BW. Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator. Proc. Natl. Acad. Sci. U.S.A. 98 2001 6045-50 [PubMed: 11353844] http://dx.doi.org/10.1073/pnas.111128198
	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

InterPro 23.1