Identification
Name:Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
Synonyms:
  • ACCase subunit beta
  • Acetyl-CoA carboxylase carboxyltransferase subunit beta
Gene Name:accD
Enzyme Class:
Biological Properties
General Function:Involved in acetyl-CoA carboxylase activity
Specific Function:Controls translation of mRNA for both itself and the alpha-subunit (accA) by binding to a probable hairpin in the 5' of the mRNA. Binding to mRNA inhibits translation; this is partially relieved by acetyl-CoA. Increasing amounts of mRNA also inhibit enzyme activity
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+Thumb+ThumbThumb+Thumb+Thumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb+Thumb
Thumb+Carboxybiotin-carboxyl-carrier proteinThumb+Holo-[carboxylase]
Acetyl-CoA + Carboxybiotin-carboxyl-carrier protein ↔ Malonyl-CoA + Holo-[carboxylase]
ReactionCard
SMPDB Reactions:
Thumb+Thumb+ThumbAdenosine diphosphate+Thumb+Thumb+Malonyl-CoA+Thumb+Thumb
a biotinylated [BCCP dimer]+Thumb+Thumbcarboxylated-biotinylated [BCCP dimer]+Thumb+Thumb+Thumb
a biotinylated [BCCP dimer] + Adenosine triphosphate + Hydrogen carbonate → carboxylated-biotinylated [BCCP dimer] + Hydrogen ion + ADP + Phosphate
ReactionCard
a biotinylated [BCCP dimer]+Thumb+Thumb+Thumb+ThumbThumb+Thumb+Thumb+carboxylated-biotinylated [BCCP dimer]
a biotinylated [BCCP dimer] + Hydrogen ion + Phosphate + ADP + Malonyl-CoAWater + Acetyl-CoA + Adenosine triphosphate + carboxylated-biotinylated [BCCP dimer]
ReactionCard
EcoCyc Reactions:
Thumb+Thumb+ThumbThumb+Thumb+Thumb+Thumb
Complex Reactions:
Thumb+Thumb+ThumbThumb+Thumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB01206Acetyl-CoAMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB03538Carbonic acidMetaboCard
ECMDB00595Hydrogen carbonateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01175Malonyl-CoAMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
acetyl-CoA carboxylase complex
macromolecular complex
protein complex
Function
acetyl-CoA carboxylase activity
catalytic activity
CoA carboxylase activity
ligase activity
ligase activity, forming carbon-carbon bonds
Process
carboxylic acid metabolic process
cellular metabolic process
fatty acid biosynthetic process
fatty acid metabolic process
metabolic process
monocarboxylic acid metabolic process
organic acid metabolic process
oxoacid metabolic process
Gene Properties
Blattner:b2316
Gene OrientationCounterclockwise
Centisome Percentage:52.40
Left Sequence End2431034
Right Sequence End2431948
Gene Sequence:
>915 bp
ATGCGTTTACCTATCTTCCTCGATACTGACCCCGGCATTGACGATGCCGTCGCCATTGCC
GCCGCGATTTTTGCACCCGAACTCGACCTGCAACTGATGACCACCGTCGCGGGTAATGTC
TCGGTTGAGAAAACTACCCGCAATGCCCTGCAACTGCTGCATTTCTGGAATGCGGAGATT
CCGCTCGCCCAAGGGGCCGCTGTGCCACTGGTACGCGCACCGCGTGATGCGGCATCTGTG
CACGGCGAATCGGGAATGGCTGGCTACGACTTTGTTGAGCACAACCGAAAGCCGCTCGGG
ATACCGGCGTTTCTGGCGATTCGGGATGCCCTGATGCGTGCACCAGAGCCTGTTACCCTG
GTGGCCATCGGCCCGTTAACCAATATTGCGCTGTTACTTTCACAATGCCCGGAATGCAAG
CCGTATATTCGCCGTCTGGTGATCATGGGTGGTTCTGCCGGACGCGGCAACTGTACGCCA
AACGCCGAGTTTAATATTGCTGCCGATCCAGAAGCTGCTGCCTGTGTCTTCCGCAGTGGT
ATTGAAATCGTCATGTGCGGTTTGGATGTCACCAATCAGGCAATATTAACTCCTGACTAT
CTCTCTACACTGCCGCAGTTAAACCGTACCGGGAAAATGCTTCACGCCCTGTTTAGCCAC
TACCGTAGCGGCAGTATGCAAAGCGGCTTGCGAATGCACGATCTCTGCGCCATCGCCTGG
CTGGTGCGCCCGGACCTGTTCACTCTCAAACCCTGTTTTGTGGCAGTGGAAACTCAGGGC
GAATTTACCTCAGGCACGACGGTGGTTGATATCGACGGTTGCCTGGGCAAGCCAGCCAAT
GTACAGGTGGCATTGGATCTGGATGTGAAAGGCTTCCAGCAGTGGGTGGCTGAGGTGCTG
GCTCTGGCGTCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:304
Protein Molecular Weight:33322
Protein Theoretical pI:8
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
MSWIERIKSNITPTRKASIPEGVWTKCDSCGQVLYRAELERNLEVCPKCDHHMRMTARNR
LHSLLDEGSLVELGSELEPKDVLKFRDSKKYKDRLASAQKETGEKDALVVMKGTLYGMPV
VAAAFEFAFMGGSMGSVVGARFVRAVEQALEDNCPLICFSASGGARMQEALMSLMQMAKT
SAALAKMQERGLPYISVLTDPTMGGVSASFAMLGDLNIAEPKALIGFAGPRVIEQTVREK
LPPGFQRSEFLIEKGAIDMIVRRPEMRLKLASILAKLMNLPAPNPEAPREGVVVPPVPDQ
EPEA
References
External Links:
ResourceLink
Uniprot ID:P0A9Q5
Uniprot Name:ACCD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321912
Ecogene ID:EG10217
Ecocyc:EG10217
ColiBase:b2316
Kegg Gene:b2316
EchoBASE ID:EB0213
CCDB:ACCD_ECOLI
BacMap:16130251
General Reference:
  • Bilder, P., Lightle, S., Bainbridge, G., Ohren, J., Finzel, B., Sun, F., Holley, S., Al-Kassim, L., Spessard, C., Melnick, M., Newcomer, M., Waldrop, G. L. (2006). "The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme." Biochemistry 45:1712-1722. Pubmed: 16460018
  • 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
  • Bognar, A. L., Osborne, C., Shane, B. (1987). "Primary structure of the Escherichia coli folC gene and its folylpolyglutamate synthetase-dihydrofolate synthetase product and regulation of expression by an upstream gene." J Biol Chem 262:12337-12343. Pubmed: 3040739
  • Freiberg, C., Brunner, N. A., Schiffer, G., Lampe, T., Pohlmann, J., Brands, M., Raabe, M., Habich, D., Ziegelbauer, K. (2004). "Identification and characterization of the first class of potent bacterial acetyl-CoA carboxylase inhibitors with antibacterial activity." J Biol Chem 279:26066-26073. Pubmed: 15066985
  • 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
  • Li, S. J., Cronan, J. E. Jr (1993). "Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis." J Bacteriol 175:332-340. Pubmed: 7678242
  • Li, S. J., Rock, C. O., Cronan, J. E. Jr (1992). "The dedB (usg) open reading frame of Escherichia coli encodes a subunit of acetyl-coenzyme A carboxylase." J Bacteriol 174:5755-5757. Pubmed: 1355086
  • Meades, G. Jr, Benson, B. K., Grove, A., Waldrop, G. L. (2010). "A tale of two functions: enzymatic activity and translational repression by carboxyltransferase." Nucleic Acids Res 38:1217-1227. Pubmed: 19965770
  • Nagano, Y., Matsuno, R., Sasaki, Y. (1991). "An essential gene of Escherichia coli that has sequence similarity to a chloroplast gene of unknown function." Mol Gen Genet 228:62-64. Pubmed: 1886618
  • Nonet, M. L., Marvel, C. C., Tolan, D. R. (1987). "The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons." J Biol Chem 262:12209-12217. Pubmed: 3040734
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837