Octanoyltransferase

Details

Name
Octanoyltransferase
Synonyms
  • 2.3.1.181
  • Lipoate-protein ligase B
  • Lipoyl/octanoyl transferase
  • Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
Gene Name
lipB
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Amino acid sequence
>lcl|BSEQ0051229|Octanoyltransferase
MTGSIRSKLSAIDVRQLGTVDYRTAWQLQRELADARVAGGADTLLLLEHPAVYTAGRRTE
THERPIDGTPVVDTDRGGKITWHGPGQLVGYPIIGLAEPLDVVNYVRRLEESLIQVCADL
GLHAGRVDGRSGVWLPGRPARKVAAIGVRVSRATTLHGFALNCDCDLAAFTAIVPCGISD
AAVTSLSAELGRTVTVDEVRATVAAAVCAALDGVLPVGDRVPSHAVPSPL
Number of residues
230
Molecular Weight
24210.415
Theoretical pI
Not Available
GO Classification
Functions
lipoyl(octanoyl) transferase activity / octanoyltransferase activity
Processes
growth / lipoate biosynthetic process / protein lipoylation
Components
cytoplasm / plasma membrane
General Function
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Specific Function
Lipoyl(octanoyl) transferase activity
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0051230|Octanoyltransferase (lipB)
GTGACGGGTTCTATCCGGTCGAAGCTGTCCGCGATCGACGTCCGCCAGCTGGGGACCGTC
GACTACCGGACCGCGTGGCAGCTACAGCGAGAGCTAGCCGACGCCCGGGTCGCCGGCGGC
GCCGACACGCTGCTGCTGTTGGAACACCCCGCGGTCTACACCGCCGGACGGCGTACCGAG
ACACACGAGCGACCCATTGACGGCACTCCGGTCGTCGACACCGACCGCGGCGGCAAGATC
ACCTGGCACGGTCCGGGGCAATTGGTCGGCTACCCGATCATCGGGCTGGCCGAACCCCTC
GACGTGGTCAATTACGTTCGGCGCCTTGAAGAATCGCTGATCCAAGTCTGCGCCGATCTG
GGCCTGCACGCCGGCCGCGTCGACGGCCGGTCCGGGGTCTGGCTGCCCGGCAGGCCGGCG
CGCAAGGTCGCGGCCATCGGTGTCCGGGTGTCGCGGGCGACGACACTGCACGGGTTTGCG
CTCAACTGCGATTGTGATTTGGCTGCCTTCACCGCCATCGTGCCATGCGGAATCAGTGAC
GCCGCAGTGACATCGCTGTCCGCCGAACTCGGCCGTACGGTCACCGTCGACGAGGTCCGC
GCGACGGTCGCCGCCGCTGTCTGCGCCGCTCTGGACGGCGTCCTACCGGTCGGTGACCGC
GTGCCCTCACACGCCGTACCATCGCCGTTATGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP9WK83
UniProtKB Entry NameLIPB_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. Ma Q, Zhao X, Nasser Eddine A, Geerlof A, Li X, Cronan JE, Kaufmann SH, Wilmanns M: The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine dyad acyltransferase. Proc Natl Acad Sci U S A. 2006 Jun 6;103(23):8662-7. Epub 2006 May 30. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03600Capric acidexperimentalunknownDetails