Biotin carboxylase (P24182)

Identification
Name:Biotin carboxylase
Synonyms:
  • Acetyl-CoA carboxylase subunit A
  • ACC
Gene Name:accC
Enzyme Class:
Biological Properties
General Function:Involved in ligase activity
Specific Function: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
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0Adenosine triphosphate + 1.0Hydrogen carbonate ↔ 1.0ADP + 1.0Hydrogen ion + 1.0Malonyl-CoA + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Acetyl-CoA + 1.0Hydrogen carbonate ↔ 1.0ADP + 1.0Phosphate + 1.0Malonyl-CoA
ReactionCard
1.0Thumb+1.0Holo-[carboxylase]+1.0Thumb+1.0Holo-[carboxylase] ↔ 1.0Thumb+1.0Thumb+1.0Carboxybiotin-carboxyl-carrier protein+1.0Carboxybiotin-carboxyl-carrier protein
1.0Adenosine triphosphate + 1.0Holo-[carboxylase] + 1.0Hydrogen carbonate + 1.0Holo-[carboxylase] ↔ 1.0ADP + 1.0Phosphate + 1.0Carboxybiotin-carboxyl-carrier protein + 1.0Carboxybiotin-carboxyl-carrier protein
ReactionCard
1.0Thumb+1.0Carboxybiotin-carboxyl-carrier protein ↔ 1.0Thumb+1.0Holo-[carboxylase]
1.0Acetyl-CoA + 1.0Carboxybiotin-carboxyl-carrier protein ↔ 1.0Malonyl-CoA + 1.0Holo-[carboxylase]
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Adenosine diphosphate+1.0Thumb+1.0Thumb+1.0Malonyl-CoA+1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0Hydrogen carbonate + 1.0Adenosine triphosphate → 1.0Adenosine diphosphate + 1.0Phosphate + 1.0Hydrogen ion + 1.0Malonyl-CoA + 1.0ADP + 1.0Malonyl-CoA
ReactionCard
1.0a biotinylated [BCCP dimer]+1.0Thumb+1.0Thumb → 1.0carboxylated-biotinylated [BCCP dimer]+1.0Thumb+1.0Thumb+1.0Thumb
1.0a biotinylated [BCCP dimer] + 1.0Adenosine triphosphate + 1.0Hydrogen carbonate → 1.0carboxylated-biotinylated [BCCP dimer] + 1.0Hydrogen ion + 1.0ADP + 1.0Phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0Adenosine triphosphate + 1.0Hydrogen carbonate ↔ 1.0ADP + 1.0Hydrogen ion + 1.0Malonyl-CoA + 1.0Phosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0biotin-[carboxyl-carrier-protein]+1.0Thumb → 1.0Thumb+1.0Thumb+1.0carboxy-biotin-[carboxyl-carrier-protein]
1.0Adenosine triphosphate + 1.0biotin-[carboxyl-carrier-protein] + 1.0Carbon dioxide → 1.0ADP + 1.0Inorganic phosphate + 1.0carboxy-biotin-[carboxyl-carrier-protein]
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01206Acetyl-CoAMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB03538Carbonic acidMetaboCard
ECMDB00595Hydrogen carbonateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01175Malonyl-CoAMetaboCard
ECMDB01429PhosphateMetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
biotin binding
catalytic activity
ligase activity
nucleoside binding
purine nucleoside binding
vitamin binding
Process
metabolic process
Gene Properties
Blattner:b3256
Gene OrientationClockwise
Centisome Percentage:73.37
Left Sequence End3403939
Right Sequence End3405288
Gene Sequence:
>1350 bp
ATGAAATTTACCCAACGTCTTAGTCTGCGCGTCAGGCTGACGCTAATCTTTTTAATTCTG
GCCTCGGTGACCTGGCTGCTTTCCAGCTTTGTCGCCTGGAAACAAACAACGGATAACGTC
GATGAATTGTTCGACACCCAACTGATGCTGTTTGCCAAGCGGTTAAGTACGCTCGATCTC
AACGAAATCAACGCGGCGGATCGCATGGCACAGACGCCAAATAGATTAAAACACGGTCAT
GTTGATGACGATGCGCTGACCTTTGCCATCTTTACCCACGACGGCAGAATGGTCCTTAAT
GATGGCGATAACGGAGAAGATATTCCCTATAGCTATCAACGGGAAGGTTTTGCTGACGGG
CAACTGGTCGGTGAAGACGATCCTTGGCGTTTTGTCTGGATGACCTCACCTGATGGCAAA
TATCGCATCGTTGTTGGCCAGGAATGGGAATACCGTGAAGACATGGCGCTGGCGATTGTT
GCCGGGCAATTGATCCCGTGGCTGGTCGCACTGCCGATTATGTTAATCATCATGATGGTA
CTACTGGGTCGTGAACTCGCGCCGCTGAACAAACTGGCGCTGGCACTACGTATGCGTGAC
CCTGACTCGGAAAAACCACTAAACGCGACTGGCGTACCCAGCGAAGTGCGGCCACTGGTT
GAGTCGCTAAATCAACTGTTCGCCCGCACACATGCGATGATGGTTCGTGAACGACGCTTT
ACCTCCGACGCAGCTCACGAACTTCGTAGCCCGTTAACGGCGCTGAAAGTGCAAACCGAA
GTTGCGCAGCTCTCTGACGATGATCCGCAGGCGCGGAAAAAAGCACTGCTCCAATTACAT
TCCGGGATCGATCGCGCTACTCGTCTGGTTGATCAACTGCTCACGCTATCGCGGCTGGAC
TCACTGGATAACCTTCAGGACGTCGCGGAGATCCCGCTTGAAGATCTCCTGCAATCGTCG
GTGATGGATATTTACCACACGGCGCAGCAGGCGAAAATTGACGTGCGACTGACACTCAAT
GCCCACAGCATCAAACGCACCGGGCAACCGCTATTGCTAAGTTTGTTGGTGCGAAATTTG
CTGGATAACGCCGTGCGCTACAGTCCACAGGGCAGCGTGGTAGACGTCACGCTGAATGCT
GATAATTTCATCGTGAGGGATAACGGCCCCGGTGTGACACCAGAGGCACTGGCGCGAATT
GGCGAACGCTTCTATCGCCCACCCGGACAAACCGCTACCGGCAGCGGGCTTGGGCTATCG
ATTGTCCAGCGAATCGCCAAATTGCATGGCATGAATGTTGAATTTGGGAATGCGGAACAA
GGTGGATTTGAGGCGAAGGTAAGCTGGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:449
Protein Molecular Weight:49320
Protein Theoretical pI:7
PDB File:1DV1
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Biotin carboxylase
MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSY
LNIPAIISAAEITGAVAIHPGYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAI
AAMKKAGVPCVPGSDGPLGDDMDKNRAIAKRIGYPVIIKASGGGGGRGMRVVRGDAELAQ
SISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVV
EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVT
EMITGVDLIKEQLRIAAGQPLSIKQEEVHVRGHAVECRINAEDPNTFLPSPGKITRFHAP
GGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIARMKNALQELIIDGIKTNVDL
QIRIMNDENFQHGGTNIHYLEKKLGLQEK
References
External Links:
ResourceLink
Uniprot ID:P24182
Uniprot Name:ACCC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675829
PDB ID:1DV1
Ecogene ID:EG10276
Ecocyc:EG10276
ColiBase:b3256
Kegg Gene:b3256
EchoBASE ID:EB0272
CCDB:ACCC_ECOLI
BacMap:16131144
General Reference:
  • Alix, J. H. (1989). "A rapid procedure for cloning genes from lambda libraries by complementation of E. coli defective mutants: application to the fabE region of the E. coli chromosome." DNA 8:779-789. Pubmed: 2575489
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kondo, H., Shiratsuchi, K., Yoshimoto, T., Masuda, T., Kitazono, A., Tsuru, D., Anai, M., Sekiguchi, M., Tanabe, T. (1991). "Acetyl-CoA carboxylase from Escherichia coli: gene organization and nucleotide sequence of the biotin carboxylase subunit." Proc Natl Acad Sci U S A 88:9730-9733. Pubmed: 1682920
  • Li, S. J., Cronan, J. E. Jr (1992). "The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase." J Biol Chem 267:855-863. Pubmed: 1370469
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Shen, Y., Chou, C. Y., Chang, G. G., Tong, L. (2006). "Is dimerization required for the catalytic activity of bacterial biotin carboxylase?" Mol Cell 22:807-818. Pubmed: 16793549
  • Thoden, J. B., Blanchard, C. Z., Holden, H. M., Waldrop, G. L. (2000). "Movement of the biotin carboxylase B-domain as a result of ATP binding." J Biol Chem 275:16183-16190. Pubmed: 10821865
  • Waldrop, G. L., Rayment, I., Holden, H. M. (1994). "Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase." Biochemistry 33:10249-10256. Pubmed: 7915138