fadD28
- Type
- protein_coding
- Name
- fadD28
- Locus Name
-
Rv2941
- Product
-
Fatty-acid-AMP ligase FadD28 (fatty-acid-AMP synthetase) (fatty-acid-AMP synthase)
- Functional Category
-
Lipid metabolism
- Location
- 3283335..3285077 (+ strand)
- Gene Length
- 1742 bp
- Nucleotides
-
TGAGTGTGCGTTCCCTTCCCGCTGCGTTGCGCGCGTGTGCGCGTCTGCAACCCCATGACCCGGCCTTCACGTTTATGGATTACGAACAGGACTGGGACGGCGTTGCGATAACCCTGACGTGGTCGCAGCTGTATCGGCGAACGCTGAATGTGGCACAGGAGCTGAGCCGTTGTGGTTCCACGGGTGACCGCGTGGTGATCTCTGCTCCGCAGGGACTCGAGTACGTCGTCGCCTTTCTCGGCGCGTTGCAGGCCGGGCGCATCGCCGTGCCGCTTTCGGTTCCACAAGGCGGCGTTACCGATGAACGTTCCGATTCGGTACTGAGTGATTCGTCGCCGGTGGCCATTCTCACTACATCGTCTGCCGTGGACGACGTCGTGCAACATGTTGCGCGGCGGCCCGGGGAATCCCCGCCATCAATTATCGAAGTTGATTTGCTCGATCTGGACGCTCCGAATGGGTATACCTTCAAAGAAGACGAGTATCCATCTACCGCGTATTTGCAATACACCTCCGGGTCCACCCGCACGCCCGCTGGCGTGGTGATGTCCCATCAGAACGTTCGGGTTAATTTCGAACAGCTGATGTCTGGCTACTTTGCGGATACCGACGGGATTCCACCGCCAAATTCCGCACTCGTATCCTGGCTACCCTTCTACCACGACATGGGTTTGGTAATAGGAATTTGCGCACCAATTCTGGGTGGATACCCCGCGGTGCTCACCAGCCCGGTGTCGTTCCTGCAGCGCCCGGCCCGGTGGATGCACTTGATGGCCAGCGATTTTCACGCCTTTTCGGCAGCACCGAATTTCGCCTTTGAACTAGCGGCACGAAGAACAACCGACGACGACATGGCCGGGCGTGACCTCGGCAACATACTGACCATCCTCAGCGGTAGCGAGCGGGTACAGGCCGCGACGATCAAGCGCTTCGCCGACCGCTTTGCTCGCTTCAATCTGCAGGAGAGGGTGATCCGGCCTTCATACGGGCTCGCAGAAGCAACGGTGTACGTGGCGACGAGCAAACCGGGTCAACCACCGGAGACCGTCGACTTCGATACTGAAAGTTTATCCGCCGGCCATGCGAAGCCGTGCGCAGGCGGCGGCGCTACATCGTTGATCAGCTACATGTTGCCGCGGTCACCGATCGTGCGGATCGTCGACTCGGACACCTGCATCGAATGTCCGGACGGAACCGTCGGCGAGATCTGGGTGCACGGCGACAACGTCGCTAATGGCTATTGGCAAAAACCCGACGAGAGTGAGCGCACGTTCGGCGGAAAGATTGTCACCCCTTCGCCGGGCACACCCGAAGGTCCTTGGCTAAGAACGGGCGACTCAGGTTTCGTCACCGATGGCAAAATGTTCATCATCGGTCGGATCAAAGATCTCCTAATTGTGTACGGACGCAACCACTCCCCCGACGACATCGAGGCAACGATCCAGGAGATCACCCGCGGGCGCTGCGCGGCGATCTCGGTTCCCGGTGACCGCAGCACCGAAAAGCTGGTCGCCATTATCGAACTCAAGAAGCGTGGCGACTCAGATCAGGACGCGATGGCTAGACTGGGCGCTATTAAACGCGAAGTCACGTCGGCTTTATCGAGTTCGCACGGTCTCAGCGTCGCGGATCTGGTTCTGGTTGCGCCTGGCTCGATCCCCATTACCACCAGCGGGAAGGTCAGGAGAGGGGCGTGTGTCGAGCAATATCGACAGGATCAATTCGCCCGCTTGGATGCCTAG
- Drug Resistance
- Mutations
- Function
- Catalyzes the activation of long-chain fatty acids (C22-24 fatty acids) as acyl-adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase Mas for further chain extension. Involved in the biosynthesis of mycoserates. Probably plays a role in host phagosome maturation arrest (PubMed:20844580). {ECO:0000269|PubMed:10573420, ECO:0000269|PubMed:11279114, ECO:0000269|PubMed:15042094, ECO:0000305|PubMed:20844580}.
- Family
-
ATP-dependent AMP-binding enzyme family
- GO
-
- growth of symbiont in host cell GO:0044119 biological_process
- DIM/DIP cell wall layer assembly GO:0071770 biological_process
- adenylyltransferase activity GO:0070566 molecular_function
- lipid biosynthetic process GO:0008610 biological_process
- ATP binding GO:0005524 molecular_function
- negative regulation by symbiont of host innate immune response GO:0052170 biological_process
- response to host immune response GO:0052572 biological_process
- plasma membrane GO:0005886 cellular_component
- ligase activity GO:0016874 molecular_function
- fatty-acyl-CoA synthase activity GO:0004321 molecular_function
- fatty acid biosynthetic process GO:0006633 biological_process
- InterPro
3E53
- Name
- Long-chain-fatty-acid--AMP ligase FadD28 (FAAL) (EC 6.2.1.-) (Acyl-AMP synthetase)
- Family
- ATP-dependent AMP-binding enzyme family
- Protein Sequence
-
MSVRSLPAALRACARLQPHDPAFTFMDYEQDWDGVAITLTWSQLYRRTLNVAQELSRCGSTGDRVVISAPQGLEYVVAFLGALQAGRIAVPLSVPQGGVTDERSDSVLSDSSPVAILTTSSAVDDVVQHVARRPGESPPSIIEVDLLDLDAPNGYTFKEDEYPSTAYLQYTSGSTRTPAGVVMSHQNVRVNFEQLMSGYFADTDGIPPPNSALVSWLPFYHDMGLVIGICAPILGGYPAVLTSPVSFLQRPARWMHLMASDFHAFSAAPNFAFELAARRTTDDDMAGRDLGNILTILSGSERVQAATIKRFADRFARFNLQERVIRPSYGLAEATVYVATSKPGQPPETVDFDTESLSAGHAKPCAGGGATSLISYMLPRSPIVRIVDSDTCIECPDGTVGEIWVHGDNVANGYWQKPDESERTFGGKIVTPSPGTPEGPWLRTGDSGFVTDGKMFIIGRIKDLLIVYGRNHSPDDIEATIQEITRGRCAAISVPGDRSTEKLVAIIELKKRGDSDQDAMARLGAIKREVTSALSSSHGLSVADLVLVAPGSIPITTSGKVRRGACVEQYRQDQFARLDA
- Mass
- 62,641 Da
- Length
- 580 Aa
Summary
Rv2941 doesn't seem to be a targeted by any drug.
-
-
R-MTU-9635470 R-MTU-9635470
R-MTU-9635470R-MTU-9635470
-
- Molecular basis of the functional divergence of fatty acyl-AMP ligase biosynthetic enzymes of Mycobacterium tuberculosis.
- J Mol Biol. 2012 Feb 17;416(2):221-38. doi: 10.1016/j.jmb.2011.12.031. Epub 2011 Dec 21.
- Mechanistic and functional insights into fatty acid activation in Mycobacterium tuberculosis.
- Nat Chem Biol. 2009 Mar;5(3):166-73. doi: 10.1038/nchembio.143. Epub 2009 Feb 1.
- 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.
- High content phenotypic cell-based visual screen identifies Mycobacterium tuberculosis acyltrehalose-containing glycolipids involved in phagosome remodeling.
- PLoS Pathog. 2010 Sep 9;6(9):e1001100. doi: 10.1371/journal.ppat.1001100.
- Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria.
- Nature. 2004 Mar 25;428(6981):441-5. doi: 10.1038/nature02384.
- Analysis of the phthiocerol dimycocerosate locus of Mycobacterium tuberculosis. Evidence that this lipid is involved in the cell wall permeability barrier.
- J Biol Chem. 2001 Jun 8;276(23):19845-54. doi: 10.1074/jbc.M100662200. Epub 2001 Mar 13.
- Complex lipid determines tissue-specific replication of Mycobacterium tuberculosis in mice.
- Nature. 1999 Nov 4;402(6757):79-83. doi: 10.1038/47042.
- targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis.
- BMC Syst Biol. 2008 Dec 19;2:109. doi: 10.1186/1752-0509-2-109.
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
- Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.