| General information | | DisProt: | DP00349 | | Name: | Bifunctional protein birA | | Synonym(s): | BIRA_ECOLI
Biotin operon repressor [domain 1]
Biotin--[acetyl-CoA-carboxylase] synthetase [domain 2]
EC=6.3.4.15
Biotin--protein ligase
| | First appeared in release: | Release 3.1 (03/31/2006) | | UniProt: | P06709 | | UniGene: | | | SwissProt: | BIRA_ECOLI | | TrEMBL: | | | NCBI (GI): | 115015 | | Source organism: | Escherichia coli | | Sequence length: | 321 | | Percent disordered: | 13% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MKDNTVPLKL IALLANGEFH SGEQLGETLG MSRAAINKHI QTLRDWGVDV FTVPGKGYSL - 60
PEPIQLLNAK QILGQLDGGS VAVLPVIDST NQYLLDRIGE LKSGDACIAE YQQAGRGRRG - 120
RKWFSPFGAN LYLSMFWRLE QGPAAAIGLS LVIGIVMAEV LRKLGADKVR VKWPNDLYLQ - 180
DRKLAGILVE LTGKTGDAAQ IVIGAGINMA MRRVEESVVN QGWITLQEAG INLDRNTLAA - 240
MLIRELRAAL ELFEQEGLAP YLSRWEKLDN FINRPVKLII GDKEIFGISR GIDKQGALLL - 300
EQDGIIKPWM GGEISLRSAE K
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| Functional narrative |
BirA acts both as a biotin-operon repressor and as the enzyme that synthesizes the corepressor, acetyl-CoA:carbon-dioxide ligase. This protein also activates biotin to form biotinyl-5'-adenylate and transfers the biotin moiety to biotin-accepting proteins.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 112 - 128 | | Length: | 17 | | Region sequence: |
QQAGRGRRGRKWFSPFG | | Modification type: | Mutant
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
| References:
- Kwon K, Streaker ED, Ruparelia S, Beckett D. "Multiple disordered loops function in corepressor-induced dimerization of the biotin repressor." J Mol Biol. 2000; 304(5): 821-33. PubMed: 11124029
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 116 - 124 | | Length: | 9 | | Region sequence: |
RGRRGRKWF | | Modification type: | | | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (glycerol (pH 6.5 / 5% (vol/vol)); phosphate 2.05 M)
| References:
- 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. 1992; 89(19): 9257-61. PubMed: 1409631
| Comments:
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| Region 3 | | Type: | Disordered | | Name: | | | Location: | 119 - 124 | | Length: | 6 | | Region sequence: |
RGRKWF | | Modification type: | | | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Unknown
| | Functional subclasses: | Substrate/ligand binding
| Detection methods:
| References:
- Streaker ED, Beckett D. "Ligand-linked structural changes in the Escherichia coli biotin repressor: the significance of surface loops for binding and allostery." J Mol Biol. 1999; 292(3): 619-32. PubMed: 10497026
| Comments:
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| Region 4 | | Type: | Disordered | | Name: | | | Location: | 140 - 146 | | Length: | 7 | | Region sequence: |
EQGPAAA | | Modification type: | Mutant
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
| References:
- Kwon K, Streaker ED, Ruparelia S, Beckett D. "Multiple disordered loops function in corepressor-induced dimerization of the biotin repressor." J Mol Biol. 2000; 304(5): 821-33. PubMed: 11124029
| Comments:
|
| Region 5 | | Type: | Disordered | | Name: | | | Location: | 194 - 197 | | Length: | 4 | | Region sequence: |
KTGD | | Modification type: | | | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
| References:
- Streaker ED, Beckett D. "Ligand-linked structural changes in the Escherichia coli biotin repressor: the significance of surface loops for binding and allostery." J Mol Biol. 1999; 292(3): 619-32. PubMed: 10497026
| Comments:
|
| Region 6 | | Type: | Disordered | | Name: | | | Location: | 194 - 199 | | Length: | 6 | | Region sequence: |
KTGDAA | | Modification type: | Mutant
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
| References:
- Kwon K, Streaker ED, Ruparelia S, Beckett D. "Multiple disordered loops function in corepressor-induced dimerization of the biotin repressor." J Mol Biol. 2000; 304(5): 821-33. PubMed: 11124029
| Comments:
|
| Region 7 | | Type: | Disordered | | Name: | | | Location: | 212 - 222 | | Length: | 11 | | Region sequence: |
RRVEESVVNQG | | Modification type: | | | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Unknown
| | Functional subclasses: | Substrate/ligand binding
| Detection methods:
| References:
- Streaker ED, Beckett D. "Ligand-linked structural changes in the Escherichia coli biotin repressor: the significance of surface loops for binding and allostery." J Mol Biol. 1999; 292(3): 619-32. PubMed: 10497026
| Comments:
|
| Region 8 | | Type: | Disordered | | Name: | | | Location: | 212 - 223 | | Length: | 12 | | Region sequence: |
RRVEESVVNQGW | | Modification type: | | | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (glycerol (pH 6.5 / 5% (vol/vol)); phosphate 2.05 M)
| References:
- 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. 1992; 89(19): 9257-61. PubMed: 1409631
| Comments:
|
| References |
- Howard PK, Shaw J, Otsuka AJ. "Nucleotide sequence of the birA gene encoding the biotin operon repressor and biotin holoenzyme synthetase functions of Escherichia coli." Gene. 1985; 35(3): 321-31. PubMed: 3899863
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