3-oxoacyl-[acyl-carrier-protein] synthase 1

Details

Name
3-oxoacyl-[acyl-carrier-protein] synthase 1
Synonyms
  • 2.3.1.41
  • Beta-ketoacyl-ACP synthase 1
  • KAS 1
Gene Name
kasA
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Amino acid sequence
>lcl|BSEQ0051274|3-oxoacyl-[acyl-carrier-protein] synthase 1
MSQPSTANGGFPSVVVTAVTATTSISPDIESTWKGLLAGESGIHALEDEFVTKWDLAVKI
GGHLKDPVDSHMGRLDMRRMSYVQRMGKLLGGQLWESAGSPEVDPDRFAVVVGTGLGGAE
RIVESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSACSSGSEAIAH
AWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTRNDEPERASRPFDKDRDGFVFG
EAGALMLIETEEHAKARGAKPLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGL
SPADIDHVNAHGTATPIGDAAEANAIRVAGCDQAAVYAPKSALGHSIGAVGALESVLTVL
TLRDGVIPPTLNYETPDPEIDLDVVAGEPRYGDYRYAVNNSFGFGGHNVALAFGRY
Number of residues
416
Molecular Weight
43315.725
Theoretical pI
Not Available
GO Classification
Functions
3-oxoacyl-[acyl-carrier-protein] synthase activity
Processes
fatty acid elongation / fatty acid elongation, saturated fatty acid / growth
Components
cell wall / cytosol / plasma membrane
General Function
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.
Specific Function
3-oxoacyl-[acyl-carrier-protein] synthase activity
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0051275|3-oxoacyl-[acyl-carrier-protein] synthase 1 (kasA)
GTGAGTCAGCCTTCCACCGCTAATGGCGGTTTCCCCAGCGTTGTGGTGACCGCCGTCACA
GCGACGACGTCGATCTCGCCGGACATCGAGAGCACGTGGAAGGGTCTGTTGGCCGGCGAG
AGCGGCATCCACGCACTCGAAGACGAGTTCGTCACCAAGTGGGATCTAGCGGTCAAGATC
GGCGGTCACCTCAAGGATCCGGTCGACAGCCACATGGGCCGACTCGACATGCGACGCATG
TCGTACGTCCAGCGGATGGGCAAGTTGCTGGGCGGACAGCTATGGGAGTCCGCCGGCAGC
CCGGAGGTCGATCCAGACCGGTTCGCCGTTGTTGTCGGCACCGGTCTAGGTGGAGCCGAG
AGGATTGTCGAGAGCTACGACCTGATGAATGCGGGCGGCCCCCGGAAGGTGTCCCCGCTG
GCCGTTCAGATGATCATGCCCAACGGTGCCGCGGCGGTGATCGGTCTGCAGCTTGGGGCC
CGCGCCGGGGTGATGACCCCGGTGTCGGCCTGTTCGTCGGGCTCGGAAGCGATCGCCCAC
GCGTGGCGTCAGATCGTGATGGGCGACGCCGACGTCGCCGTCTGCGGCGGTGTCGAAGGA
CCCATCGAGGCGCTGCCCATCGCGGCGTTCTCCATGATGCGGGCCATGTCGACCCGCAAC
GACGAGCCTGAGCGGGCCTCCCGGCCGTTCGACAAGGACCGCGACGGCTTTGTGTTCGGC
GAGGCCGGTGCGCTGATGCTCATCGAGACGGAGGAGCACGCCAAAGCCCGTGGCGCCAAG
CCGTTGGCCCGATTGCTGGGTGCCGGTATCACCTCGGACGCCTTTCATATGGTGGCGCCC
GCGGCCGATGGTGTTCGTGCCGGTAGGGCGATGACTCGCTCGCTGGAGCTGGCCGGGTTG
TCGCCGGCGGACATCGACCACGTCAACGCGCACGGCACGGCGACGCCTATCGGCGACGCC
GCGGAGGCCAACGCCATCCGCGTCGCCGGTTGTGATCAGGCCGCGGTGTACGCGCCGAAG
TCTGCGCTGGGCCACTCGATCGGCGCGGTCGGTGCGCTCGAGTCGGTGCTCACGGTGCTG
ACGCTGCGCGACGGCGTCATCCCGCCGACCCTGAACTACGAGACACCCGATCCCGAGATC
GACCTTGACGTCGTCGCCGGCGAACCGCGCTATGGCGATTACCGCTACGCAGTCAACAAC
TCGTTCGGGTTCGGCGGCCACAATGTGGCGCTTGCCTTCGGGCGTTACTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP9WQD9
UniProtKB Entry NameFAB1_MYCTU
General References
  1. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
  2. Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [Article]
  3. Luckner SR, Machutta CA, Tonge PJ, Kisker C: Crystal structures of Mycobacterium tuberculosis KasA show mode of action within cell wall biosynthesis and its inhibition by thiolactomycin. Structure. 2009 Jul 15;17(7):1004-13. doi: 10.1016/j.str.2009.04.012. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB043024-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-OneexperimentalunknownDetails