Malonyl CoA-acyl carrier protein transacylase (P0AAI9)

Identification
Name:Malonyl CoA-acyl carrier protein transacylase
Synonyms:
  • MCT
Gene Name:fabD
Enzyme Class:
Biological Properties
General Function:Involved in transferase activity
Specific Function:Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein]
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Acyl-carrier protein+1.0Acyl-carrier protein ↔ 1.0Thumb+1.0Malonyl-[acyl-carrier protein]+1.0Malonyl-[acyl-carrier protein]
1.0Malonyl-CoA + 1.0Acyl-carrier protein + 1.0Acyl-carrier protein ↔ 1.0Coenzyme A + 1.0Malonyl-[acyl-carrier protein] + 1.0Malonyl-[acyl-carrier protein]
ReactionCard
SMPDB Reactions:
1.0Malonyl-CoA+1.0a holo-[acyl-carrier protein] +1.0Thumb → 1.0Thumb+1.0a malonyl-[acp]
1.0Malonyl-CoA + 1.0a holo-[acyl-carrier protein]  + 1.0Malonyl-CoA → 1.0Coenzyme A + 1.0a malonyl-[acp]
ReactionCard
1.0Malonyl-CoA+1.0a holo-[acyl-carrier protein]+1.0Thumb → 1.0Thumb+1.0a malonyl-[acp]
1.0Malonyl-CoA + 1.0a holo-[acyl-carrier protein] + 1.0Malonyl-CoA → 1.0Coenzyme A + 1.0a malonyl-[acp]
ReactionCard
Complex Reactions:
1.0acyl carrier protein+1.0Thumb ↔ 1.0Thumb+1.0Malonyl-[acyl-carrier protein]
1.0acyl carrier protein + 1.0Malonyl-CoA ↔ 1.0Coenzyme A + 1.0Malonyl-[acyl-carrier protein]
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01423Coenzyme AMetaboCard
ECMDB01175Malonyl-CoAMetaboCard
ECMDB21427Myristic acidMetaboCard
ECMDB21442Palmitoleic acidMetaboCard
ECMDB21428Stearic acidMetaboCard
ECMDB21443Vaccenic acidMetaboCard
GO Classification:
Function
acyltransferase activity
binding
catalytic activity
fatty acid synthase activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
[acyl-carrier-protein] S-malonyltransferase activity
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:b1092
Gene OrientationClockwise
Centisome Percentage:24.76
Left Sequence End1148951
Right Sequence End1149880
Gene Sequence:
>930 bp
ATGATTCAGCAAGGAGATCTCATGCCGCAGTCCGCGTTGTTCACGGGAATCATTCCCCCT
GTCTCCACCATTTTTACCGCCGACGGCCAGCTCGATAAGCCGGGCACCGCCGCGCTGATC
GACGATCTGATCAAAGCAGGCGTTGACGGCCTGTTCTTCCTGGGCAGCGGTGGCGAGTTC
TCCCAGCTCGGCGCCGAAGAGCGTAAAGCCATTGCCCGCTTTGCTATCGATCATGTCGAT
CGTCGCGTGCCGGTGCTGATCGGCACCGGCGGCACCAACGCCCGGGAAACCATCGAACTC
AGCCAGCACGCGCAGCAGGCGGGCGCGGACGGCATCGTGGTGATCAACCCCTACTACTGG
AAAGTGTCGGAAGCGAACCTGATCCGCTATTTCGAGCAGGTGGCCGACAGCGTCACGCTG
CCGGTGATGCTCTATAACTTCCCGGCGCTGACCGGGCAGGATCTGACTCCGGCGCTGGTG
AAAACCCTCGCCGACTCGCGCAGCAATATTATCGGCATCAAAGACACCATCGACTCCGTC
GCCCACCTGCGCAGCATGATCCATACCGTCAAAGGTGCCCATCCGCACTTCACCGTGCTC
TGCGGCTACGACGATCATCTGTTCAATACCCTGCTGCTCGGCGGCGACGGGGCGATATCG
GCGAGCGGCAACTTTGCCCCGCAGGTGTCGGTGAATCTTCTGAAAGCCTGGCGCGACGGG
GACGTGGCGAAAGCGGCCGGGTATCATCAGACCTTGCTGCAAATTCCGCAGATGTATCAG
CTGGATACGCCGTTTGTGAACGTGATTAAAGAGGCGATCGTGCTCTGCGGTCGTCCTGTC
TCCACGCACGTGCTGCCGCCCGCCTCGCCGCTGGACGAGCCGCGCAAGGCGCAGCTGAAA
ACCCTGCTGCAACAGCTCAAGCTTTGCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:309
Protein Molecular Weight:32417
Protein Theoretical pI:5
PDB File:1MLA
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Malonyl CoA-acyl carrier protein transacylase
MTQFAFVFPGQGSQTVGMLADMAASYPIVEETFAEASAALGYDLWALTQQGPAEELNKTW
QTQPALLTASVALYRVWQQQGGKAPAMMAGHSLGEYSALVCAGVIDFADAVRLVEMRGKF
MQEAVPEGTGAMAAIIGLDDASIAKACEEAAEGQVVSPVNFNSPGQVVIAGHKEAVERAG
AACKAAGAKRALPLPVSVPSHCALMKPAADKLAVELAKITFNAPTVPVVNNVDVKCETNG
DAIRDALVRQLYNPVQWTKSVEYMAAQGVEHLYEVGPGKVLTGLTKRIVDTLTASALNEP
SAMAAALEL
References
External Links:
ResourceLink
Uniprot ID:P0AAI9
Uniprot Name:FABD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674412
PDB ID:1MLA
Ecogene ID:EG11317
Ecocyc:EG11317
ColiBase:b1092
Kegg Gene:b1092
EchoBASE ID:EB1293
CCDB:FABD_ECOLI
BacMap:16129055
General Reference:
  • 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
  • Bouquin, N., Tempete, M., Holland, I. B., Seror, S. J. (1995). "Resistance to trifluoroperazine, a calmodulin inhibitor, maps to the fabD locus in Escherichia coli." Mol Gen Genet 246:628-637. Pubmed: 7700236
  • 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
  • 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
  • Magnuson, K., Oh, W., Larson, T. J., Cronan, J. E. Jr (1992). "Cloning and nucleotide sequence of the fabD gene encoding malonyl coenzyme A-acyl carrier protein transacylase of Escherichia coli." FEBS Lett 299:262-266. Pubmed: 1339356
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Rawlings, M., Cronan, J. E. Jr (1992). "The gene encoding Escherichia coli acyl carrier protein lies within a cluster of fatty acid biosynthetic genes." J Biol Chem 267:5751-5754. Pubmed: 1556094
  • Serre, L., Verbree, E. C., Dauter, Z., Stuitje, A. R., Derewenda, Z. S. (1995). "The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-A resolution. Crystal structure of a fatty acid synthase component." J Biol Chem 270:12961-12964. Pubmed: 7768883
  • Verwoert, I. I., Verbree, E. C., van der Linden, K. H., Nijkamp, H. J., Stuitje, A. R. (1992). "Cloning, nucleotide sequence, and expression of the Escherichia coli fabD gene, encoding malonyl coenzyme A-acyl carrier protein transacylase." J Bacteriol 174:2851-2857. Pubmed: 1314802