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
Functions
3-oxoacyl-[acyl-carrier-protein] synthase activity / beta-ketoacyl-acyl-carrier-protein synthase III activity
Processes
fatty acid biosynthetic process
Components
cytoplasm
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
ResourceLink
UniProtKB IDQ820T1
UniProtKB Entry NameFABH_ENTFA
GenBank Protein ID29342120
GenBank Gene IDAE016830
General References
  1. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB074292-({[4-bromo-3-(diethylsulfamoyl)phenyl]carbonyl}amino)benzoic acidexperimentalunknownDetails