fadD32
- Type
- protein_coding
- Name
- fadD32
- Locus Name
-
Rv3801c
- Product
-
Fatty-acid-AMP ligase FadD32 (fatty-acid-AMP synthetase) (fatty-acid-AMP synthase). Also shown to have acyl-ACP ligase activity.
- Functional Category
-
None
- Location
- 4261153..4263066 (- strand)
- Gene Length
- 1913 bp
- Nucleotides
-
ATGTTTGTGACAGGAGAGAGTGGGATGGCGTACCACAACCCGTTCATCGTGAATGGAAAGATCAGGTTCCCAGCCAACACCAACCTGGTTCGTCACGTCGAAAAGTGGGCGAAGGTTCGTGGCGACAAGCTGGCCTACCGGTTCCTGGACTTTTCCACCGAACGAGACGGTGTCGCGCGCGACATCTTGTGGTCTGACTTCAGCGCGCGCAACCGTGCGGTGGGAGCCCGCCTGCAGCAAGTCACCCAGCCGGGTGACCGCGTCGCCATCCTGTGCCCGCAGAACCTGGACTACCTCATCTCCTTCTTCGGCGCCCTCTACTCCGGCCGCATTGCGGTGCCGTTGTTCGACCCGGCCGAGCCGGGGCACGTCGGTCGGTTACACGCGGTGCTCGACGACTGTGCCCCGTCGACGATCCTGACCACCACCGACTCCGCCGAAGGGGTCCGCAAGTTCATCCGGGCCCGATCGGCCAAGGAGCGCCCGCGCGTCATTGCCGTCGACGCGGTGCCCACCGAAGTCGCCGCCACCTGGCAGCAGCCCGAGGCCAACGAGGAAACCGTCGCGTACTTGCAGTACACGTCGGGTTCCACCCGCATACCGAGCGGCGTGCAGATCACCCATCTGAACCTGCCCACCAATGTGGTGCAGGTGCTCAATGCCCTGGAAGGACAGGAAGGCGACCGCGGGGTCAGCTGGCTCCCGTTCTTCCACGACATGGGTCTGATCACGGTGCTGCTGGCGTCGGTGCTAGGCCACAGCTTCACCTTTATGACGCCCGCGGCGTTCGTGCGGCGGCCCGGTCGCTGGATCCGCGAGCTCGCCCGCAAGCCCGGAGAAACCGGTGGCACCTTCTCTGCGGCGCCGAACTTCGCATTCGAACACGCCGCGGTGCGCGGTGTGCCTCGAGACGACGAGCCGCCGCTGGACCTGAGCAACGTCAAGGGCATCCTCAACGGCAGCGAGCCGGTGTCGCCGGCGTCGATGCGCAAGTTCTTCGAAGCATTTGCGCCGTACGGTTTGAAGCAGACCGCCGTCAAGCCGTCCTATGGGCTAGCGGAGGCCACGCTGTTCGTCTCGACCACGCCGATGGACGAGGTGCCCACCGTGATCCACGTGGACCGCGACGAGCTGAACAACCAGCGGTTCGTTGAGGTGGCCGCCGATGCACCCAACGCCGTCGCCCAGGTCTCTGCGGGCAAGGTCGGGGTCAGCGAATGGGCGGTCATCGTCGACGCCGACACGGCCAGCGAACTGCCGGACGGACAGATCGGTGAGATCTGGCTGCACGGCAACAACTTGGGTACCGGTTATTGGGGCAAAGAAGAAGAGTCCGCCCAGACCTTCAAGAACATCCTCAAATCGCGGATCAGCGAGTCGCGCGCCGAGGGCGCCCCAGACGACGCGCTGTGGGTGCGTACCGGCGACTACGGCACCTACTTCAAGGACCACCTCTACATAGCCGGCCGGATCAAGGACCTCGTCATCATCGACGGCCGCAATCACTACCCACAGGATCTCGAGTGCACGGCGCAGGAGTCGACCAAGGCGTTGCGGGTTGGCTACGCGGCGGCCTTCTCGGTTCCGGCCAACCAGCTTCCTCAGACAGTGTTCGACGACTCGCACGCCGGGCTGAAATTCGACCCCGAGGACACCTCCGAGCAGCTGGTGATCGTCGGCGAACGGGCGGCCGGCACGCATAAGCTCGACCACCAGCCCATCGTCGATGACATCCGGGCGGCCATCGCCGTCGGGCATGGGGTGACCGTGCGTGACGTCCTGCTGGTGTCGGCCGGCACGATTCCGCGAACCTCCAGCGGCAAGATCGGCCGCCGCGCCTGCCGTGCGGCCTACCTCGACGGCAGCCTGCGCAGTGGCGTGGGTTCCCCGACGGTCTTCGCCACTTCGGACTG
- Drug Resistance
- Mutations
- Function
- Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase (PKS) for further chain extension. {ECO:0000269|PubMed:15042094}.
- Family
-
ATP-dependent AMP-binding enzyme family
- GO
-
- mycolate cell wall layer assembly GO:0071769 biological_process
- Actinobacterium-type cell wall biogenesis GO:0071766 biological_process
- adenylyltransferase activity GO:0070566 molecular_function
- lipid biosynthetic process GO:0008610 biological_process
- cell wall GO:0005618 cellular_component
- ATP binding GO:0005524 molecular_function
- plasma membrane GO:0005886 cellular_component
- ligase activity GO:0016874 molecular_function
- fatty acid biosynthetic process GO:0006633 biological_process
- InterPro
5HM3
- Name
- Long-chain-fatty-acid--AMP ligase FadD32 (FAAL) (EC 6.2.1.-) (Acyl-AMP synthetase)
- Family
- ATP-dependent AMP-binding enzyme family
- Protein Sequence
-
MFVTGESGMAYHNPFIVNGKIRFPANTNLVRHVEKWAKVRGDKLAYRFLDFSTERDGVARDILWSDFSARNRAVGARLQQVTQPGDRVAILCPQNLDYLISFFGALYSGRIAVPLFDPAEPGHVGRLHAVLDDCAPSTILTTTDSAEGVRKFIRARSAKERPRVIAVDAVPTEVAATWQQPEANEETVAYLQYTSGSTRIPSGVQITHLNLPTNVVQVLNALEGQEGDRGVSWLPFFHDMGLITVLLASVLGHSFTFMTPAAFVRRPGRWIRELARKPGETGGTFSAAPNFAFEHAAVRGVPRDDEPPLDLSNVKGILNGSEPVSPASMRKFFEAFAPYGLKQTAVKPSYGLAEATLFVSTTPMDEVPTVIHVDRDELNNQRFVEVAADAPNAVAQVSAGKVGVSEWAVIVDADTASELPDGQIGEIWLHGNNLGTGYWGKEEESAQTFKNILKSRISESRAEGAPDDALWVRTGDYGTYFKDHLYIAGRIKDLVIIDGRNHYPQDLECTAQESTKALRVGYAAAFSVPANQLPQTVFDDSHAGLKFDPEDTSEQLVIVGERAAGTHKLDHQPIVDDIRAAIAVGHGVTVRDVLLVSAGTIPRTSSGKIGRRACRAAYLDGSLRSGVGSPTVFATSD
- Mass
- 69,232 Da
- Length
- 637 Aa
Summary
Rv3801c doesn't seem to be a targeted by any drug.
Rv3801c doesn't seem to be involved in any pathway.
- 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.
- 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.
- 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.
- Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria.
- Nature. 2004 Mar 25;428(6981):441-5. doi: 10.1038/nature02384.
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
- Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.