DB code: T00113

CATH domain 1.10.10.10 : Arc Repressor Mutant, subunit A
3.30.930.10 : BirA Bifunctional Protein; domain 2 Catalytic domain
2.30.30.100 : SH3 type barrels.
E.C. 6.3.4.15
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
1.10.10.10 : Arc Repressor Mutant, subunit A D00510 D00452 D00077 D00517 T00055
3.30.930.10 : BirA Bifunctional Protein; domain 2 S00413 D00291 D00293 D00294 D00295 M00049

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Includes RefSeq Pfam
P06709 Bifunctional protein birA
None Biotin operon repressor
Biotin--{acetyl-CoA-carboxylase} synthetase
EC 6.3.4.15
Biotin--protein ligase
NP_418404.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491483.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF02237 (BPL_C)
PF03099 (BPL_LplA_LipB)
PF08279 (HTH_11)
[Graphical View]

KEGG enzyme name
biotin---[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

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P06709 BIRA_ECOLI ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon- dioxide ligase (ADP-forming)]. Monomer.

KEGG Pathways
Map code Pathways E.C.
MAP00780 Biotin metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C00002 C00120 C04735 C02188 C00020 C00013 C04681 C06250 C05921
E.C.
Compound Magnesium ATP Biotin Apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] Protein lysine AMP Pyrophosphate [Acetyl-CoA:carbon-dioxide ligase (ADP-forming)] Holo-[carboxylase] Biotinyl-5'-AMP
Type divalent metal (Ca2+, Mg2+) amine group,nucleotide amide group,amine group,fatty acid,sulfide group peptide/protein amine group,lipid,peptide/protein amine group,nucleotide phosphate group/phosphate ion peptide/protein amide group,lipid,peptide/protein,sulfide group
ChEBI 18420
15422
15956
16027
29888
PubChem 888
5957
171548
6083
1023
21961011
1biaA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bibA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hxdA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hxdB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1biaA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bibA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:BTN Unbound Unbound Unbound Unbound Unbound Unbound
1hxdA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:BTN Unbound Unbound Unbound Unbound Unbound Unbound
1hxdB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:BTN Unbound Unbound Unbound Unbound Unbound Unbound
1biaA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bibA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hxdA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hxdB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [1] & [4]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1biaA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1bibA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1hxdA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1hxdB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1biaA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ; ;LYS 183 invisible 116-124
1bibA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 118;;LYS 183 invisible 119-124
1hxdA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 118;ARG 121;LYS 183
1hxdB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 118;ARG 121;LYS 183
1biaA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1bibA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1hxdA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1hxdB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
p.9259
[4]
Fig.1, p.360 2

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)
Medline ID 93028443
PubMed ID 1409631
Journal Proc Natl Acad Sci U S A
Year 1992
Volume 89
Pages 9257-61
Authors Wilson KP, Shewchuk LM, Brennan RG, Otsuka AJ, Matthews BW
Title Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains.
Related PDB 1bia 1bib
Related UniProtKB P06709
[2]
Resource
Comments
Medline ID
PubMed ID 9750231
Journal Methods Enzymol
Year 1998
Volume 295
Pages 424-50
Authors Beckett D
Title Energetic methods to study bifunctional biotin operon repressor.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 9880519
Journal J Biol Chem
Year 1999
Volume 274
Pages 1449-57
Authors Chapman-Smith A, Morris TW, Wallace JC, Cronan JE Jr
Title 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.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 10470036
Journal Trends Biochem Sci
Year 1999
Volume 24
Pages 359-63
Authors Chapman-Smith A, Cronan JE Jr
Title The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 10981714
Journal FEBS Lett
Year 2000
Volume 479
Pages 93-8
Authors Reche PA, Howard MJ, Broadhurst RW, Perham RN
Title Heteronuclear NMR studies of the specificity of the post-translational modification of biotinyl domains by biotinyl protein ligase.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 11353844
Journal Proc Natl Acad Sci U S A
Year 2001
Volume 98
Pages 6045-50
Authors Weaver LH, Kwon K, Beckett D, Matthews BW
Title Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator.
Related PDB 1hxd
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 11714929
Journal Protein Sci
Year 2001
Volume 10
Pages 2608-17
Authors Chapman-Smith A, Mulhern TD, Whelan F, Cronan JE Jr, Wallace JC
Title The C-terminal domain of biotin protein ligase from E. coli is required for catalytic activity.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 11714930
Journal Protein Sci
Year 2001
Volume 10
Pages 2618-22
Authors Weaver LH, Kwon K, Beckett D, Matthews BW
Title Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 15033356
Journal J Mol Biol
Year 2004
Volume 337
Pages 857-69
Authors Brown PH, Cronan JE, Grotli M, Beckett D
Title The biotin repressor: modulation of allostery by corepressor analogs.
Related PDB
Related UniProtKB

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.

Created Updated
2004-08-01 2009-02-26