3-oxoacyl-[acyl-carrier-protein] synthase 3 (P0A6R0)

Identification
Name:3-oxoacyl-[acyl-carrier-protein] synthase 3
Synonyms:
  • 3-oxoacyl-[acyl-carrier-protein] synthase III
  • Beta-ketoacyl-ACP synthase III
  • KAS III
  • EcFabH
Gene Name:fabH
Enzyme Class:
Biological Properties
General Function:Involved in 3-oxoacyl-[acyl-carrier-protein] synthase activity
Specific Function:Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Acyl-carrier protein ↔ 1.0Thumb+1.0Acetyl-[acyl-carrier protein]
1.0Acetyl-CoA + 1.0Acyl-carrier protein ↔ 1.0Coenzyme A + 1.0Acetyl-[acyl-carrier protein]
ReactionCard
1.0Acetyl-[acyl-carrier protein]+1.0Malonyl-[acyl-carrier protein] ↔ 1.0Acetoacetyl-[acp]+1.0Thumb+1.0Acyl-carrier protein
1.0Acetyl-[acyl-carrier protein] + 1.0Malonyl-[acyl-carrier protein] ↔ 1.0Acetoacetyl-[acp] + 1.0Carbon dioxide + 1.0Acyl-carrier protein
ReactionCard
1.0Thumb+1.0Malonyl-[acyl-carrier protein] ↔ 1.0Acetoacetyl-[acp]+1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0Malonyl-[acyl-carrier protein] ↔ 1.0Acetoacetyl-[acp] + 1.0Coenzyme A + 1.0Carbon dioxide
ReactionCard
SMPDB Reactions:
1.0a malonyl-[acp]+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0acetoacetyl-[acp]
1.0a malonyl-[acp] + 1.0Hydrogen ion + 1.0Acetyl-CoA → 1.0Carbon dioxide + 1.0Coenzyme A + 1.0acetoacetyl-[acp]
ReactionCard
1.0Thumb+1.0a holo-[acyl-carrier protein] → 1.0Thumb+1.0an acetyl-[acp]
1.0Acetyl-CoA + 1.0a holo-[acyl-carrier protein] → 1.0Coenzyme A + 1.0an acetyl-[acp]
ReactionCard
Complex Reactions:
1.0acyl carrier protein+1.0Thumb ↔ 1.0Acetyl-ACP+1.0Thumb
1.0acyl carrier protein + 1.0Acetyl-CoA ↔ 1.0Acetyl-ACP + 1.0Coenzyme A
ReactionCard
1.0Thumb+1.0Thumb+1.0Malonyl-[acyl-carrier protein] → 1.0Acetoacetyl-ACP+1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0Hydrogen ion + 1.0Malonyl-[acyl-carrier protein] → 1.0Acetoacetyl-ACP + 1.0Carbon dioxide + 1.0Coenzyme A
ReactionCard
1.0Thumb+1.0Malonyl-[acyl-carrier protein]+1.0malonyl-CoA methyl ester → 1.0Thumb+1.0Thumb+3.0-Oxo-glutaryl-[acyl-carrier protein] methyl ester
1.0Hydrogen ion + 1.0Malonyl-[acyl-carrier protein] + 1.0malonyl-CoA methyl ester → 1.0Carbon dioxide + 1.0Coenzyme A + 3.0-Oxo-glutaryl-[acyl-carrier protein] methyl ester
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01206Acetyl-CoAMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB21538Heptadecenoic acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21506Margaric acidMetaboCard
GO Classification:
Function
3-oxoacyl-[acyl-carrier-protein] synthase activity
acyltransferase activity
catalytic activity
fatty acid synthase activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
Process
carboxylic acid metabolic process
cellular metabolic process
fatty acid biosynthetic process
fatty acid metabolic process
lipid biosynthetic process
lipid metabolic process
metabolic process
monocarboxylic acid metabolic process
organic acid metabolic process
oxoacid metabolic process
primary metabolic process
Gene Properties
Blattner:b1091
Gene OrientationClockwise
Centisome Percentage:24.74
Left Sequence End1147982
Right Sequence End1148935
Gene Sequence:
>954 bp
ATGACGGACAAATTGACCTCCCTTCGTCAGTACACCACCGTAGTGGCCGACACTGGGGAC
ATCGCGGCAATGAAGCTGTATCAACCGCAGGATGCCACAACCAACCCTTCTCTCATTCTT
AACGCAGCGCAGATTCCGGAATACCGTAAGTTGATTGATGATGCTGTCGCCTGGGCGAAA
CAGCAGAGCAACGATCGCGCGCAGCAGATCGTGGACGCGACCGACAAACTGGCAGTAAAT
ATTGGTCTGGAAATCCTGAAACTGGTTCCGGGCCGTATCTCAACTGAAGTTGATGCGCGT
CTTTCCTATGACACCGAAGCGTCAATTGCGAAAGCAAAACGCCTGATCAAACTCTACAAC
GATGCTGGTATTAGCAACGATCGTATTCTGATCAAACTGGCTTCTACCTGGCAGGGTATC
CGTGCTGCAGAACAGCTGGAAAAAGAAGGCATCAACTGTAACCTGACCCTGCTGTTCTCC
TTCGCTCAGGCTCGTGCTTGTGCGGAAGCGGGCGTGTTCCTGATCTCGCCGTTTGTTGGC
CGTATTCTTGACTGGTACAAAGCGAATACCGATAAGAAAGAGTACGCTCCGGCAGAAGAT
CCGGGCGTGGTTTCTGTATCTGAAATCTACCAGTACTACAAAGAGCACGGTTATGAAACC
GTGGTTATGGGCGCAAGCTTCCGTAACATCGGCGAAATTCTGGAACTGGCAGGCTGCGAC
CGTCTGACCATCGCACCGGCACTGCTGAAAGAGCTGGCGGAGAGCGAAGGGGCTATCGAA
CGTAAACTGTCTTACACCGGCGAAGTGAAAGCGCGTCCGGCGCGTATCACTGAGTCCGAG
TTCCTGTGGCAGCACAACCAGGATCCAATGGCAGTAGATAAACTGGCGGAAGGTATCCGT
AAGTTTGCTATTGACCAGGAAAAACTGGAAAAAATGATCGGCGATCTGCTGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:317
Protein Molecular Weight:33515
Protein Theoretical pI:5
PDB File:1HNK
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>3-oxoacyl-[acyl-carrier-protein] synthase 3
MYTKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAAT
RAIEMAGIEKDQIGLIVVATTSATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALS
VADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDGAGAAVLAASEEPGIISTHLH
ADGSYGELLTLPNADRVNPENSIHLTMAGNEVFKVAVTELAHIVDETLAANNLDRSQLDW
LVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVL
LEAFGGGFTWGSALVRF
References
External Links:
ResourceLink
Uniprot ID:P0A6R0
Uniprot Name:FABH_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321899
PDB ID:1HNK
Ecogene ID:EG10277
Ecocyc:EG10277
ColiBase:b1091
Kegg Gene:b1091
EchoBASE ID:EB0273
CCDB:FABH_ECOLI
BacMap:16129054
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
  • Davies, C., Heath, R. J., White, S. W., Rock, C. O. (2000). "The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli." Structure 8:185-195. Pubmed: 10673437
  • 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
  • Heath, R. J., Rock, C. O. (1996). "Inhibition of beta-ketoacyl-acyl carrier protein synthase III (FabH) by acyl-acyl carrier protein in Escherichia coli." J Biol Chem 271:10996-11000. Pubmed: 8631920
  • Khandekar, S. S., Gentry, D. R., Van Aller, G. S., Warren, P., Xiang, H., Silverman, C., Doyle, M. L., Chambers, P. A., Konstantinidis, A. K., Brandt, M., Daines, R. A., Lonsdale, J. T. (2001). "Identification, substrate specificity, and inhibition of the Streptococcus pneumoniae beta-ketoacyl-acyl carrier protein synthase III (FabH)." J Biol Chem 276:30024-30030. Pubmed: 11375394
  • 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
  • Oh, W., Larson, T. J. (1992). "Physical locations of genes in the rne (ams)-rpmF-plsX-fab region of the Escherichia coli K-12 chromosome." J Bacteriol 174:7873-7874. Pubmed: 1447160
  • 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
  • Qiu, X., Janson, C. A., Konstantinidis, A. K., Nwagwu, S., Silverman, C., Smith, W. W., Khandekar, S., Lonsdale, J., Abdel-Meguid, S. S. (1999). "Crystal structure of beta-ketoacyl-acyl carrier protein synthase III. A key condensing enzyme in bacterial fatty acid biosynthesis." J Biol Chem 274:36465-36471. Pubmed: 10593943
  • Qiu, X., Janson, C. A., Smith, W. W., Head, M., Lonsdale, J., Konstantinidis, A. K. (2001). "Refined structures of beta-ketoacyl-acyl carrier protein synthase III." J Mol Biol 307:341-356. Pubmed: 11243824
  • Tsay, J. T., Oh, W., Larson, T. J., Jackowski, S., Rock, C. O. (1992). "Isolation and characterization of the beta-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12." J Biol Chem 267:6807-6814. Pubmed: 1551888
  • 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
  • Zhang, Y. M., Rao, M. S., Heath, R. J., Price, A. C., Olson, A. J., Rock, C. O., White, S. W. (2001). "Identification and analysis of the acyl carrier protein (ACP) docking site on beta-ketoacyl-ACP synthase III." J Biol Chem 276:8231-8238. Pubmed: 11078736