Biotin carboxylase

Details

Name
Biotin carboxylase
Synonyms
  • 6.3.4.14
  • ACC
  • Acetyl-CoA carboxylase subunit A
  • fabG
Gene Name
accC
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0012892|Biotin carboxylase
MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSY
LNIPAIISAAEITGAVAIHPGYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAI
AAMKKAGVPCVPGSDGPLGDDMDKNRAIAKRIGYPVIIKASGGGGGRGMRVVRGDAELAQ
SISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVV
EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVT
EMITGVDLIKEQLRIAAGQPLSIKQEEVHVRGHAVECRINAEDPNTFLPSPGKITRFHAP
GGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIARMKNALQELIIDGIKTNVDL
QIRIMNDENFQHGGTNIHYLEKKLGLQEK
Number of residues
449
Molecular Weight
49320.32
Theoretical pI
7.12
GO Classification
Functions
acetyl-CoA carboxylase activity / ATP binding / biotin carboxylase activity / metal ion binding
Processes
fatty acid biosynthetic process / malonyl-CoA biosynthetic process / negative regulation of fatty acid biosynthetic process
Components
cytoplasm / cytosol
General Function
Metal ion binding
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0012893|Biotin carboxylase (accC)
ATGCTGGATAAAATTGTTATTGCCAACCGCGGCGAGATTGCATTGCGTATTCTTCGTGCC
TGTAAAGAACTGGGCATCAAGACTGTCGCTGTGCACTCCAGCGCGGATCGCGATCTAAAA
CACGTATTACTGGCAGATGAAACGGTCTGTATTGGCCCTGCTCCGTCAGTAAAAAGTTAT
CTGAACATCCCGGCAATCATCAGCGCCGCTGAAATCACCGGCGCAGTAGCAATCCATCCG
GGTTACGGCTTCCTCTCCGAGAACGCCAACTTTGCCGAGCAGGTTGAACGCTCCGGCTTT
ATCTTCATTGGCCCGAAAGCAGAAACCATTCGCCTGATGGGCGACAAAGTATCCGCAATC
GCGGCGATGAAAAAAGCGGGCGTCCCTTGCGTACCGGGTTCTGACGGCCCGCTGGGCGAC
GATATGGATAAAAACCGTGCCATTGCTAAACGCATTGGTTATCCGGTGATTATCAAAGCC
TCCGGCGGCGGCGGCGGTCGCGGTATGCGCGTAGTGCGCGGCGACGCTGAACTGGCACAA
TCCATCTCCATGACCCGTGCGGAAGCGAAAGCTGCTTTCAGCAACGATATGGTTTACATG
GAGAAATACCTGGAAAATCCTCGCCACGTCGAGATTCAGGTACTGGCTGACGGTCAGGGC
AACGCTATCTATCTGGCGGAACGTGACTGCTCCATGCAACGCCGCCACCAGAAAGTGGTC
GAAGAAGCGCCAGCACCGGGCATTACCCCGGAACTGCGTCGCTACATCGGCGAACGTTGC
GCTAAAGCGTGTGTTGATATCGGCTATCGCGGTGCAGGTACTTTCGAGTTCCTGTTCGAA
AACGGCGAGTTCTATTTCATCGAAATGAACACCCGTATTCAGGTAGAACACCCGGTTACA
GAAATGATCACCGGCGTTGACCTGATCAAAGAACAGCTGCGTATCGCTGCCGGTCAACCG
CTGTCGATCAAGCAAGAAGAAGTTCACGTTCGCGGCCATGCGGTGGAATGTCGTATCAAC
GCCGAAGATCCGAACACCTTCCTGCCAAGTCCGGGCAAAATCACCCGTTTCCACGCACCT
GGCGGTTTTGGCGTACGTTGGGAGTCTCATATCTACGCGGGCTACACCGTACCGCCGTAC
TATGACTCAATGATCGGTAAGCTGATTTGCTACGGTGAAAACCGTGACGTGGCGATTGCC
CGCATGAAGAATGCGCTGCAGGAGCTGATCATCGACGGTATCAAAACCAACGTTGATCTG
CAGATCCGCATCATGAATGACGAGAACTTCCAGCATGGTGGCACTAACATCCACTATCTG
GAGAAAAAACTCGGTCTTCAGGAAAAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP24182
UniProtKB Entry NameACCC_ECOLI
GenBank Protein ID145896
GenBank Gene IDM79446
General References
  1. Kondo H, Shiratsuchi K, Yoshimoto T, Masuda T, Kitazono A, Tsuru D, Anai M, Sekiguchi M, Tanabe T: Acetyl-CoA carboxylase from Escherichia coli: gene organization and nucleotide sequence of the biotin carboxylase subunit. Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9730-3. [Article]
  2. Li SJ, Cronan JE Jr: The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase. J Biol Chem. 1992 Jan 15;267(2):855-63. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
  6. Alix JH: 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. 1989 Dec;8(10):779-89. [Article]
  7. Waldrop GL, Rayment I, Holden HM: Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase. Biochemistry. 1994 Aug 30;33(34):10249-56. [Article]
  8. Thoden JB, Blanchard CZ, Holden HM, Waldrop GL: Movement of the biotin carboxylase B-domain as a result of ATP binding. J Biol Chem. 2000 May 26;275(21):16183-90. [Article]
  9. Shen Y, Chou CY, Chang GG, Tong L: Is dimerization required for the catalytic activity of bacterial biotin carboxylase? Mol Cell. 2006 Jun 23;22(6):807-18. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB080743-(3-Methyl-2-buten-1-yl)-3H-purin-6-amineexperimentalunknownDetails
DB080754-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amineexperimentalunknownDetails
DB080764-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amineexperimentalunknownDetails
DB081446-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamineexperimentalunknownDetails
DB081456-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINEexperimentalunknownDetails
DB081467-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amineexperimentalunknownDetails
DB08314(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONEexperimentalunknownDetails
DB083152-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDEexperimentalunknownDetails
DB083164-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-oneexperimentalunknownDetails
DB083175-methyl-6-phenylquinazoline-2,4-diamineexperimentalunknownDetails
DB083186-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamineexperimentalunknownDetails