| General information | | DisProt: | DP00415 | | Name: | Biotin carboxyl carrier protein of acetyl-CoA carboxylase | | Synonym(s): | BCCP_ECO57
BCCP
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P0ABE0 | | UniGene: | | | SwissProt: | BCCP_ECO57 | | TrEMBL: | | | NCBI (GI): | 78099821 | | Source organism: | Escherichia coli | | Sequence length: | 156 | | Percent disordered: | 18% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MDIRKIKKLI ELVEESGISE LEISEGEESV RISRAAPAAS FPVMQQAYAA PMMQQPAQSN - 60
AAAPATVPSM EAPAAAEISG HIVRSPMVGT FYRTPSPDAK AFIEVGQKVN VGDTLCIVEA - 120
MKMMNQIEAD KSGTVKAILV ESGQPVEFDE PLVVIE
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| Functional narrative |
Biotin carboxyl carrier protein (BCCP) is the small biotinylated subunit of Escherichia coli acetyl-CoA carboxylase, the enzyme that catalyzes the first committed step of fatty acid synthesis. This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
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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: | 49 - 76 | | Length: | 28 | | Region sequence: |
AAPMMQQPAQSNAAAPATVPSMEAPAAA | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Entropic chain
| | Functional subclasses: | Flexible linkers/spacers
| Detection methods:
- Nuclear magnetic resonance (NMR)
| References:
- Cronan JE Jr. "Interchangeable enzyme modules. Functional replacement of the essential linker of the biotinylated subunit of acetyl-CoA carboxylase with a linker from the lipoylated subunit of pyruvate dehydrogenase." J Biol Chem. 2002; 277(25): 22520-7. PubMed: 11956202
| Comments:
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| References |
- Choi-Rhee E, Cronan JE. "The biotin carboxylase-biotin carboxyl carrier protein complex of Escherichia coli acetyl-CoA carboxylase." J Biol Chem. 2003; 278(33): 30806-12. PubMed: 12794081
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