Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (P0ABD5)

Identification
Name:Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
Synonyms:
  • ACCase subunit alpha
  • Acetyl-CoA carboxylase carboxyltransferase subunit alpha
Gene Name:accA
Enzyme Class:
Biological Properties
General Function:Involved in acetyl-CoA carboxylase activity
Specific Function:Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA
Cellular Location:Cytoplasm
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+1.0Carboxybiotin-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+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Acetyl-CoA + 1.0Carbonic acid → 1.0ADP + 1.0Inorganic phosphate + 1.0Malonyl-CoA
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01206Acetyl-CoAMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB03538Carbonic acidMetaboCard
ECMDB00595Hydrogen carbonateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01175Malonyl-CoAMetaboCard
ECMDB01429PhosphateMetaboCard
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:b0185
Gene OrientationClockwise
Centisome Percentage:4.50
Left Sequence End208621
Right Sequence End209580
Gene Sequence:
>960 bp
ATGAGTCTGAATTTCCTTGATTTTGAACAGCCGATTGCAGAGCTGGAAGCGAAAATCGAT
TCTCTGACTGCGGTTAGCCGTCAGGATGAGAAACTGGATATTAACATCGATGAAGAAGTG
CATCGTCTGCGTGAAAAAAGCGTAGAACTGACACGTAAAATCTTCGCCGATCTCGGTGCA
TGGCAGATTGCGCAACTGGCACGCCATCCACAGCGTCCTTATACCCTGGATTACGTTCGC
CTGGCATTTGATGAATTTGACGAACTGGCTGGCGACCGCGCGTATGCAGACGATAAAGCT
ATCGTCGGTGGTATCGCCCGTCTCGATGGTCGTCCGGTGATGATCATTGGTCATCAAAAA
GGTCGTGAAACCAAAGAAAAAATTCGCCGTAACTTTGGTATGCCAGCGCCAGAAGGTTAC
CGCAAAGCACTGCGTCTGATGCAAATGGCTGAACGCTTTAAGATGCCTATCATCACCTTT
ATCGACACCCCGGGGGCTTATCCTGGCGTGGGCGCAGAAGAGCGTGGTCAGTCTGAAGCC
ATTGCACGCAACCTGCGTGAAATGTCTCGCCTCGGCGTACCGGTAGTTTGTACGGTTATC
GGTGAAGGTGGTTCTGGCGGTGCGCTGGCGATTGGCGTGGGCGATAAAGTGAATATGCTG
CAATACAGCACCTATTCCGTTATCTCGCCGGAAGGTTGTGCGTCCATTCTGTGGAAGAGC
GCCGACAAAGCGCCGCTGGCGGCTGAAGCGATGGGTATCATTGCTCCGCGTCTGAAAGAA
CTGAAACTGATCGACTCCATCATCCCGGAACCACTGGGTGGTGCTCACCGTAACCCGGAA
GCGATGGCGGCATCGTTGAAAGCGCAACTGCTGGCGGATCTGGCCGATCTCGACGTGTTA
AGCACTGAAGATTTAAAAAATCGTCGTTATCAGCGCCTGATGAGCTACGGTTACGCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:319
Protein Molecular Weight:35241
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGA
WQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQK
GRETKEKIRRNFGMPAPEGYRKALRLMQMAERFKMPIITFIDTPGAYPGVGAEERGQSEA
IARNLREMSRLGVPVVCTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKS
ADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRNPEAMAASLKAQLLADLADLDVL
STEDLKNRRYQRLMSYGYA
References
External Links:
ResourceLink
Uniprot ID:P0ABD5
Uniprot Name:ACCA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674373
Ecogene ID:EG11647
Ecocyc:EG11647
ColiBase:b0185
Kegg Gene:b0185
EchoBASE ID:EB1600
CCDB:ACCA_ECOLI
BacMap:16128178
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
  • 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
  • Kikuchi, Y., Kojima, H., Tanaka, T., Takatsuka, Y., Kamio, Y. (1997). "Characterization of a second lysine decarboxylase isolated from Escherichia coli." J Bacteriol 179:4486-4492. Pubmed: 9226257
  • Li, S. J., Cronan, J. E. Jr (1992). "The genes encoding the two carboxyltransferase subunits of Escherichia coli acetyl-CoA carboxylase." J Biol Chem 267:16841-16847. Pubmed: 1355089
  • 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
  • Tomasiewicz, H. G., McHenry, C. S. (1987). "Sequence analysis of the Escherichia coli dnaE gene." J Bacteriol 169:5735-5744. Pubmed: 3316192
  • Yamamoto, Y., Miwa, Y., Miyoshi, K., Furuyama, J., Ohmori, H. (1997). "The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme." Genes Genet Syst 72:167-172. Pubmed: 9339543