T00113
type: Enzyme
cath: Arc Repressor Mutant, subunit A
cath: BirA Bifunctional Protein; domain 2
cath: SH3 type barrels.
ec: https://purl.uniprot.org/enzyme/6.3.4.15
uniprot: P06709
kegg enzyme: biotin---[acetyl-CoA-carboxylase] ligase
kegg enzyme: biotin-[acetyl-CoA carboxylase] synthetase
kegg enzyme: biotin-[acetyl coenzyme A carboxylase] synthetase
kegg enzyme: acetyl coenzyme A holocarboxylase synthetase
kegg enzyme: acetyl CoA holocarboxylase synthetase
kegg enzyme: biotin:apocarboxylase ligase
kegg enzyme: Biotin holoenzyme synthetase
kegg enzyme: HCS
kegg pathway: Biotin metabolism
kegg cofactor: Magnesium
kegg substrate: ATP
kegg substrate: Biotin
kegg substrate: Apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
kegg substrate: Protein lysine
kegg product: AMP
kegg product: Pyrophosphate
kegg product: [Acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
kegg product: Holo-[carboxylase]
kegg intermediate: Biotinyl-5'-AMP
pdb: 1biaA01
pdb: 1bibA01
pdb: 1hxdA01
pdb: 1hxdB01
pdb: 1biaA02
pdb: 1bibA02
pdb: 1hxdA02
pdb: 1hxdB02
pdb: 1biaA03
pdb: 1bibA03
pdb: 1hxdA03
pdb: 1hxdB03
pdb bound state: Unbound
  compound: ATP
  pdb: 1biaA01
pdb bound state: Unbound
  compound: ATP
  pdb: 1bibA01
pdb bound state: Unbound
  compound: ATP
  pdb: 1hxdA01
pdb bound state: Unbound
  compound: ATP
  pdb: 1hxdB01
pdb bound state: Unbound
  compound: ATP
  pdb: 1biaA02
pdb bound state: Unbound
  compound: ATP
  pdb: 1bibA02
pdb bound state: Unbound
  compound: ATP
  pdb: 1hxdA02
pdb bound state: Unbound
  compound: ATP
  pdb: 1hxdB02
pdb bound state: Unbound
  compound: ATP
  pdb: 1biaA03
pdb bound state: Unbound
  compound: ATP
  pdb: 1bibA03
pdb bound state: Unbound
  compound: ATP
  pdb: 1hxdA03
pdb bound state: Unbound
  compound: ATP
  pdb: 1hxdB03
pdb bound state: Unbound
  compound: Biotin
  pdb: 1biaA01
pdb bound state: Unbound
  compound: Biotin
  pdb: 1bibA01
pdb bound state: Unbound
  compound: Biotin
  pdb: 1hxdA01
pdb bound state: Unbound
  compound: Biotin
  pdb: 1hxdB01
pdb bound state: Unbound
  compound: Biotin
  pdb: 1biaA02
pdb bound state: Unbound
  compound: Biotin
  pdb: 1biaA03
pdb bound state: Unbound
  compound: Biotin
  pdb: 1bibA03
pdb bound state: Unbound
  compound: Biotin
  pdb: 1hxdA03
pdb bound state: Unbound
  compound: Biotin
  pdb: 1hxdB03
pdb bound state: Unbound
  compound: Apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
  pdb: 1biaA01
pdb bound state: Unbound
  compound: Apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
  pdb: 1bibA01
pdb bound state: Unbound
  compound: Apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
  pdb: 1hxdA01
pdb bound state: Unbound
  compound: Apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
  pdb: 1hxdB01
pdb bound state: Unbound
  compound: Apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
  pdb: 1biaA02
pdb bound state: Unbound
  compound: Apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
  pdb: 1bibA02
pdb bound state: Unbound
  compound: Apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
  pdb: 1hxdA02
pdb bound state: Unbound
  compound: Apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
  pdb: 1hxdB02
pdb bound state: Unbound
  compound: Apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
  pdb: 1biaA03
pdb bound state: Unbound
  compound: Apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
  pdb: 1bibA03
active site residues resources: Energetic methods to study bifunctional biotin operon repressor.
active site residues resources: Heteronuclear NMR studies of the specificity of the post-translational modification of biotinyl domains by biotinyl protein ligase.
references: Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains.
references: Energetic methods to study bifunctional biotin operon repressor.
references: Molecular recognition in a post-translational modification of exceptional specificity. Mutants of the biotinylated domain of acetyl-CoA carboxylase defective in recognition by biotin protein ligase.
references: The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity.
references: Heteronuclear NMR studies of the specificity of the post-translational modification of biotinyl domains by biotinyl protein ligase.
references: Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator.
references: The C-terminal domain of biotin protein ligase from E. coli is required for catalytic activity.
references: Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor.
references: The biotin repressor: modulation of allostery by corepressor analogs.
comment: This protein is bifunctional, acting both as a biotin-transferring enzyme and as a transcriptional regulator (see [1]). As the biotin-transferring enzyme, this protein catalyzes two successive reactions. The first reaction is transfer of adenylate from ATP to the carboxylate of biotin, which results in the formation of biotinyl-5'-AMP, releasing pyrophosphate. The second reaction is transfer of the biotin moiety from the intermediate, biotinyl-5'-AMP, to the correct lysine residue of protein substrate, acetyl-CoA carboxylase. However, the detailed mechanism of catalysis has not been elucidated.

Arc Repressor Mutant, subunit A
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.10.10

BirA Bifunctional Protein; domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.930.10
catalytic domain: index.html

SH3 type barrels.
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.30.30.100

Biotin metabolism
type: KeggPathway
references: KEGG:MAP00780

Magnesium
type: KeggCofactor
references: KEGG:C00305
compound type: divalent metal (Ca2+, Mg2+)
references: CHEBI:18420
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

ATP
type: KeggSubstrate
references: KEGG:C00002
compound type: amine group
compound type: nucleotide
references: CHEBI:15422
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Biotin
type: KeggSubstrate
references: KEGG:C00120
compound type: amide group
compound type: amine group
compound type: fatty acid
compound type: sulfide group
references: CHEBI:15956
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
type: KeggSubstrate
references: KEGG:C04735
compound type: peptide/protein

Protein lysine
type: KeggSubstrate
references: KEGG:C02188
compound type: amine group
compound type: lipid
compound type: peptide/protein

AMP
type: KeggProduct
references: KEGG:C00020
compound type: amine group
compound type: nucleotide
references: CHEBI:16027
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Pyrophosphate
type: KeggProduct
references: KEGG:C00013
compound type: phosphate group/phosphate ion
references: CHEBI:29888
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

[Acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
type: KeggProduct
references: KEGG:C04681
compound type: peptide/protein

Holo-[carboxylase]
type: KeggProduct
references: KEGG:C06250
compound type: amide group
compound type: lipid
compound type: peptide/protein
compound type: sulfide group

Biotinyl-5'-AMP
type: KeggIntermediate
references: KEGG:C05921

1biaA02
type: Pdb
references: 1bia
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bia
catalytic residue: ; ;LYS 183
comment: invisible 116-124

1bibA02
type: Pdb
references: 1bib
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bib
catalytic residue: ARG 118; ;LYS 183
comment: invisible 119-124

1hxdA02
type: Pdb
references: 1hxd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hxd
catalytic residue: ARG 118;ARG 121;LYS 183

1hxdB02
type: Pdb
references: 1hxd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hxd
catalytic residue: ARG 118;ARG 121;LYS 183

Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)
medline id: 93028443
references: http://www.ncbi.nlm.nih.gov/pubmed/1409631
journal: Proc Natl Acad Sci U S A
volume: 89
pages: 9257-61
published year: 1992
authors:
  item: Wilson KP
  item: Shewchuk LM
  item: Brennan RG
  item: Otsuka AJ
  item: Matthews BW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P06709

Energetic methods to study bifunctional biotin operon repressor.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9750231
journal: Methods Enzymol
volume: 295
pages: 424-50
published year: 1998
authors:
  item: Beckett D

Molecular recognition in a post-translational modification of exceptional specificity. Mutants of the biotinylated domain of acetyl-CoA carboxylase defective in recognition by biotin protein ligase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9880519
journal: J Biol Chem
volume: 274
pages: 1449-57
published year: 1999
authors:
  item: Chapman-Smith A
  item: Morris TW
  item: Wallace JC
  item: Cronan JE Jr

The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10470036
journal: Trends Biochem Sci
volume: 24
pages: 359-63
published year: 1999
authors:
  item: Chapman-Smith A
  item: Cronan JE Jr

Heteronuclear NMR studies of the specificity of the post-translational modification of biotinyl domains by biotinyl protein ligase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10981714
journal: FEBS Lett
volume: 479
pages: 93-8
published year: 2000
authors:
  item: Reche PA
  item: Howard MJ
  item: Broadhurst RW
  item: Perham RN

Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11353844
journal: Proc Natl Acad Sci U S A
volume: 98
pages: 6045-50
published year: 2001
authors:
  item: Weaver LH
  item: Kwon K
  item: Beckett D
  item: Matthews BW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The C-terminal domain of biotin protein ligase from E. coli is required for catalytic activity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11714929
journal: Protein Sci
volume: 10
pages: 2608-17
published year: 2001
authors:
  item: Chapman-Smith A
  item: Mulhern TD
  item: Whelan F
  item: Cronan JE Jr
  item: Wallace JC

Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11714930
journal: Protein Sci
volume: 10
pages: 2618-22
published year: 2001
authors:
  item: Weaver LH
  item: Kwon K
  item: Beckett D
  item: Matthews BW

The biotin repressor: modulation of allostery by corepressor analogs.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15033356
journal: J Mol Biol
volume: 337
pages: 857-69
published year: 2004
authors:
  item: Brown PH
  item: Cronan JE
  item: Grotli M
  item: Beckett D

ReferenceForCatalyticMechanism
reference index: 1
reference section: p.9259

ReferenceForCatalyticMechanism
reference index: 4
reference section: Fig.1, p.360
reference step: 2