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
- Functionsacetyl-CoA carboxylase activity / ATP binding / biotin carboxylase activity / metal ion bindingProcessesfatty acid biosynthetic process / malonyl-CoA biosynthetic process / negative regulation of fatty acid biosynthetic processComponentscytoplasm / 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
Resource Link UniProtKB ID P24182 UniProtKB Entry Name ACCC_ECOLI GenBank Protein ID 145896 GenBank Gene ID M79446 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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 ID Name Drug group Pharmacological action? Actions Details DB08074 3-(3-Methyl-2-buten-1-yl)-3H-purin-6-amine experimental unknown Details DB08075 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine experimental unknown Details DB08076 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine experimental unknown Details DB08144 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine experimental unknown Details DB08145 6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE experimental unknown Details DB08146 7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine experimental unknown Details DB08314 (2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE experimental unknown Details DB08315 2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE experimental unknown Details DB08316 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one experimental unknown Details DB08317 5-methyl-6-phenylquinazoline-2,4-diamine experimental unknown Details DB08318 6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine experimental unknown Details