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
- Gene Name
- fabH
- Organism
- Enterococcus faecalis (strain ATCC 700802 / V583)
- Amino acid sequence
>lcl|BSEQ0012698|3-oxoacyl-[acyl-carrier-protein] synthase 3 MKNYARISCTSRYVPENCVTNHQLSEMMDTSDEWIHSRTGISERRIVTQENTSDLCHQVA KQLLEKSGKQASEIDFILVATVTPDFNMPSVACQVQGAIGATEAFAFDISAACSGFVYAL SMAEKLVLSGRYQTGLVIGGETFSKMLDWTDRSTAVLFGDGAAGVLIEAAETPHFLNEKL QADGQRWAALTSGYTINESPFYQGHKQASKTLQMEGRSIFDFAIKDVSQNILSLVTDETV DYLLLHQANVRIIDKIARKTKISREKFLTNMDKYGNTSAASIPILLDEAVENGTLILGSQ QRVVLTGFGGGLTWGSLLLTL
- Number of residues
- 321
- Molecular Weight
- 35181.65
- Theoretical pI
- 5.19
- 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. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0012699|3-oxoacyl-[acyl-carrier-protein] synthase 3 (fabH) ATGAAGAATTATGCACGAATTAGTTGTACAAGCCGTTATGTTCCAGAGAATTGTGTCACG AATCACCAACTGAGTGAAATGATGGATACCTCTGATGAATGGATACATTCGCGAACAGGC ATTAGTGAACGTCGCATCGTTACGCAAGAAAATACGTCTGATTTATGTCATCAAGTCGCA AAACAGTTATTGGAAAAATCTGGAAAGCAAGCAAGTGAGATTGACTTTATTTTAGTTGCA ACAGTGACACCAGATTTCAATATGCCTTCTGTTGCTTGCCAAGTGCAAGGCGCAATTGGC GCCACTGAGGCCTTTGCTTTTGACATCAGTGCAGCGTGTTCTGGTTTTGTCTATGCCTTA AGCATGGCAGAAAAACTAGTCTTAAGTGGTCGTTATCAAACAGGTCTAGTAATTGGTGGC GAAACATTTTCCAAAATGTTGGATTGGACCGATCGCTCCACAGCGGTGCTTTTCGGTGAT GGGGCTGCCGGCGTCTTGATTGAAGCGGCTGAGACACCGCATTTTCTAAATGAAAAATTA CAAGCAGATGGACAACGGTGGGCGGCTTTAACGTCAGGCTACACGATCAACGAAAGTCCT TTTTATCAGGGGCATAAGCAGGCGAGTAAGACGCTACAGATGGAAGGACGTAGTATTTTT GATTTTGCGATTAAAGATGTTTCACAAAATATTTTATCACTCGTGACGGACGAAACCGTG GATTATCTTCTACTACATCAAGCAAATGTGCGCATTATCGATAAAATTGCACGTAAGACG AAGATTTCCCGCGAGAAGTTTTTAACGAATATGGATAAATATGGCAATACCTCAGCTGCT AGTATTCCTATTTTGTTGGATGAAGCAGTTGAAAATGGGACCTTAATTTTAGGTTCCCAA CAACGCGTGGTGCTAACAGGATTTGGCGGCGGCTTAACATGGGGCTCACTGCTCCTAACG CTGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q820T1 UniProtKB Entry Name FABH_ENTFA GenBank Protein ID 29342120 GenBank Gene ID AE016830 - General References
- Paulsen IT, Banerjei L, Myers GS, Nelson KE, Seshadri R, Read TD, Fouts DE, Eisen JA, Gill SR, Heidelberg JF, Tettelin H, Dodson RJ, Umayam L, Brinkac L, Beanan M, Daugherty S, DeBoy RT, Durkin S, Kolonay J, Madupu R, Nelson W, Vamathevan J, Tran B, Upton J, Hansen T, Shetty J, Khouri H, Utterback T, Radune D, Ketchum KA, Dougherty BA, Fraser CM: Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis. Science. 2003 Mar 28;299(5615):2071-4. [Article]