3-oxoacyl-[acyl-carrier-protein] synthase 3
Details
- Name
- 3-oxoacyl-[acyl-carrier-protein] synthase 3
- Synonyms
- 2.3.1.180
- 3-oxoacyl-[acyl-carrier-protein] synthase III
- Beta-ketoacyl-ACP synthase III
- KAS III
- zhuH
- Gene Name
- fabH
- Organism
- Streptomyces lividans
- Amino acid sequence
>lcl|BSEQ0016865|3-oxoacyl-[acyl-carrier-protein] synthase 3 MPGLRVPERRFSRVLGVGSYRPRREVSNKEVCTWIDSTEEWIETRTGIRSRRIAEPDETI QVMGVAASRRALEHAGVDPAEIDLVVVSTMTNFVHTPPLSVAIAHELGADNAGGFDLSAA CAGFCHALSIAADAVESGGSRHVLVVATERMTDVIDLADRSLSFLFGDGAGAAVVGPSDV PGIGPVVRGIDGTGLGSLHMSSSWDQYVEDPSVGRPALVMDGKRVFRWAVADVVPAAREA LEVAGLTVGDLVAFVPHQANLRIIDVLVDRLGVPEHVVVSRDAEDTGNTSSASVALALDR LVRSGAVPGGGPALMIGFGAGLSYAGQALLLPDPPSTPA
- Number of residues
- 339
- Molecular Weight
- 35391.78
- Theoretical pI
- 4.77
- GO Classification
- Functions3-oxoacyl-[acyl-carrier-protein] synthase activity / beta-ketoacyl-acyl-carrier-protein synthase III activityProcessesfatty acid biosynthetic processComponentscytoplasm
- General Function
- Beta-ketoacyl-acyl-carrier-protein synthase iii 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 preference for butyryl-CoA and can tolerate branched substrates. Can also prime acyl-CoA. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids. Involved in the biosynthesis of R1128 polyketide.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0005255|1020 bp ATGCCCGGACTTCGGGTTCCCGAGCGGCGTTTCAGCCGTGTTCTCGGGGTCGGTTCGTAC CGGCCCCGCCGTGAGGTGAGCAACAAGGAGGTGTGCACCTGGATCGACTCGACGGAGGAG TGGATCGAGACGCGCACCGGGATCAGGTCGCGGCGGATCGCCGAGCCGGACGAGACGATC CAGGTGATGGGGGTGGCCGCGAGCCGCCGCGCGCTGGAGCACGCCGGCGTGGATCCGGCC GAGATCGACCTGGTCGTGGTCTCCACGATGACCAACTTCGTGCACACGCCGCCGCTTTCG GTCGCGATCGCGCACGAGCTGGGTGCCGACAACGCCGGCGGGTTCGACCTGTCGGCGGCG TGCGCGGGGTTCTGCCACGCGTTGTCGATCGCGGCGGACGCGGTGGAGTCCGGCGGTTCG CGGCACGTGCTCGTGGTGGCGACGGAGCGGATGACCGACGTGATCGACCTGGCGGACCGG AGCCTGTCGTTCCTGTTCGGCGACGGCGCCGGCGCGGCCGTGGTCGGCCCGTCCGACGTG CCCGGCATCGGTCCGGTGGTGCGCGGCATCGACGGCACCGGCCTGGGCTCGCTGCACATG AGCAGTTCGTGGGACCAGTACGTCGAGGACCCCTCGGTGGGCCGGCCGGCGCTGGTGATG GACGGCAAGCGGGTGTTCCGCTGGGCGGTCGCGGACGTCGTCCCGGCGGCCCGCGAGGCG CTCGAGGTGGCCGGCCTGACCGTCGGGGACCTGGTGGCGTTCGTCCCGCACCAGGCCAAC CTGCGGATCATCGACGTGCTGGTGGACCGGCTCGGCGTGCCGGAGCACGTGGTCGTCTCG CGCGACGCGGAGGACACCGGCAACACCTCGTCGGCGTCGGTGGCCCTGGCCCTGGACCGG CTGGTGCGCTCCGGCGCGGTGCCCGGCGGCGGGCCCGCGCTGATGATCGGTTTCGGCGCC GGGCTGAGCTACGCGGGCCAGGCTCTACTGCTTCCCGACCCGCCGTCCACTCCGGCTTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q9F6D4 UniProtKB Entry Name FABH_STRLI GenBank Gene ID AF293442 - General References
- Marti T, Hu Z, Pohl NL, Shah AN, Khosla C: Cloning, nucleotide sequence, and heterologous expression of the biosynthetic gene cluster for R1128, a non-steroidal estrogen receptor antagonist. Insights into an unusual priming mechanism. J Biol Chem. 2000 Oct 27;275(43):33443-8. [Article]
- Meadows ES, Khosla C: In vitro reconstitution and analysis of the chain initiating enzymes of the R1128 polyketide synthase. Biochemistry. 2001 Dec 11;40(49):14855-61. [Article]
- Pan H, Tsai Sc, Meadows ES, Miercke LJ, Keatinge-Clay AT, O'Connell J, Khosla C, Stroud RM: Crystal structure of the priming beta-ketosynthase from the R1128 polyketide biosynthetic pathway. Structure. 2002 Nov;10(11):1559-68. [Article]