EzCatDB: T00113
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DB codeT00113
CATH domainDomain 11.10.10.10 : Arc Repressor Mutant, subunit A
Domain 23.30.930.10 : BirA Bifunctional Protein; domain 2Catalytic domain
Domain 32.30.30.100 : SH3 type barrels.
E.C.6.3.4.15

CATH domainRelated DB codes (homologues)
1.10.10.10 : Arc Repressor Mutant, subunit AD00510,D00452,D00077,D00517,T00055
3.30.930.10 : BirA Bifunctional Protein; domain 2S00413,D00291,D00293,D00294,D00295,M00049

Enzyme Name
UniProtKBKEGG

P06709
Protein nameBifunctional protein birAbiotin---[acetyl-CoA-carboxylase] ligase
biotin-[acetyl-CoA carboxylase] synthetase
biotin-[acetyl coenzyme A carboxylase] synthetase
acetyl coenzyme A holocarboxylase synthetase
acetyl CoA holocarboxylase synthetase
biotin:apocarboxylase ligase
Biotin holoenzyme synthetase
HCS
SynonymsNone
IncludesBiotin operon repressor
Biotin--{acetyl-CoA-carboxylase} synthetase
   EC 6.3.4.15
Biotin--protein ligase
RefSeqNP_418404.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491483.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PfamPF02237 (BPL_C)
PF03099 (BPL_LplA_LipB)
PF08279 (HTH_11)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00780Biotin metabolism

UniProtKB:Accession NumberP06709
Entry nameBIRA_ECOLI
ActivityATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon- dioxide ligase (ADP-forming)].
SubunitMonomer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00305C00002C00120C04735C02188C00020C00013C04681C06250C05921
CompoundMagnesiumATPBiotinApo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]Protein lysineAMPPyrophosphate[Acetyl-CoA:carbon-dioxide ligase (ADP-forming)]Holo-[carboxylase]Biotinyl-5'-AMP
Typedivalent metal (Ca2+, Mg2+)amine group,nucleotideamide group,amine group,fatty acid,sulfide grouppeptide/proteinamine group,lipid,peptide/proteinamine group,nucleotidephosphate group/phosphate ionpeptide/proteinamide group,lipid,peptide/protein,sulfide group
ChEBI18420
15422
15956


16027
29888



PubChem888
5957
171548


6083
21961011
1023



                  
1biaA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
1bibA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
1hxdA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
1hxdB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
1biaA02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
1bibA02UnboundUnboundBound:BTNUnboundUnboundUnboundUnboundUnboundUnbound 
1hxdA02UnboundUnboundBound:BTNUnboundUnboundUnboundUnboundUnboundUnbound 
1hxdB02UnboundUnboundBound:BTNUnboundUnboundUnboundUnboundUnboundUnbound 
1biaA03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
1bibA03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
1hxdA03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
1hxdB03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 

Active-site residues
resource
literature [1] & [4]
pdbCatalytic residuescomment
          
1biaA01 
 
1bibA01 
 
1hxdA01 
 
1hxdB01 
 
1biaA02       ;       ;LYS 183
invisible 116-124
1bibA02ARG 118;       ;LYS 183
invisible 119-124
1hxdA02ARG 118;ARG 121;LYS 183
 
1hxdB02ARG 118;ARG 121;LYS 183
 
1biaA03 
 
1bibA03 
 
1hxdA03 
 
1hxdB03 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]p.9259
[4]Fig.1, p.3602

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)
Medline ID93028443
PubMed ID1409631
JournalProc Natl Acad Sci U S A
Year1992
Volume89
Pages9257-61
AuthorsWilson KP, Shewchuk LM, Brennan RG, Otsuka AJ, Matthews BW
TitleEscherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains.
Related PDB1bia,1bib
Related UniProtKBP06709
[2]
PubMed ID9750231
JournalMethods Enzymol
Year1998
Volume295
Pages424-50
AuthorsBeckett D
TitleEnergetic methods to study bifunctional biotin operon repressor.
[3]
PubMed ID9880519
JournalJ Biol Chem
Year1999
Volume274
Pages1449-57
AuthorsChapman-Smith A, Morris TW, Wallace JC, Cronan JE Jr
TitleMolecular 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.
[4]
PubMed ID10470036
JournalTrends Biochem Sci
Year1999
Volume24
Pages359-63
AuthorsChapman-Smith A, Cronan JE Jr
TitleThe enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity.
[5]
PubMed ID10981714
JournalFEBS Lett
Year2000
Volume479
Pages93-8
AuthorsReche PA, Howard MJ, Broadhurst RW, Perham RN
TitleHeteronuclear NMR studies of the specificity of the post-translational modification of biotinyl domains by biotinyl protein ligase.
[6]
PubMed ID11353844
JournalProc Natl Acad Sci U S A
Year2001
Volume98
Pages6045-50
AuthorsWeaver LH, Kwon K, Beckett D, Matthews BW
TitleCorepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator.
Related PDB1hxd
[7]
PubMed ID11714929
JournalProtein Sci
Year2001
Volume10
Pages2608-17
AuthorsChapman-Smith A, Mulhern TD, Whelan F, Cronan JE Jr, Wallace JC
TitleThe C-terminal domain of biotin protein ligase from E. coli is required for catalytic activity.
[8]
PubMed ID11714930
JournalProtein Sci
Year2001
Volume10
Pages2618-22
AuthorsWeaver LH, Kwon K, Beckett D, Matthews BW
TitleCompeting protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor.
[9]
PubMed ID15033356
JournalJ Mol Biol
Year2004
Volume337
Pages857-69
AuthorsBrown PH, Cronan JE, Grotli M, Beckett D
TitleThe biotin repressor: modulation of allostery by corepressor analogs.

comments
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.

createdupdated
2004-08-012009-02-26


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Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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